wanglab/gogpt-training-data huggingface dataset:
Protein: Succinate receptor 1 (G-protein coupled receptor 91) (Q99MT6)
Organism: Mus musculus (Mouse)
Function: Receptor for succinate.
Subcellular location: Cell membrane {ECO:0000305|PubMed:29735652}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-neuropeptide Y
- Hydroxycarboxylic acid receptor 2
Sequence:
MAQNLSCENWLATEAILNKYYLSAFYAIEFIFGLLGNVTVVFGYLFCMKNWNSSNVYLFNLSISDFAFLCTLPILIKSYANDKGTYGDVLCISNRYVLHTNLYTSILFLTFISMDRYLLMKYPFREHFLQKKEFAILISLAVWALVTLEVLPMLTFINSVPKEEGSNCIDYASSGNPEHNLIYSLCLTLLGFLIPLSVMCFFYYKMVVFLKRRSQQQATALPLDKPQRLVVLAVVIFSILFTPYHIMRNLRIASRLDSWPQGCTQKAIKSIYTLTRPLAFLNSAINPIFYFLMGDHYREMLISKFRQYFKSLTSFRT
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (EC 3.2.1.113) (Man(9)-alpha-mannosidase) (Man9-mannosidase) (Mannosidase alpha class 1A member 1) (Processing alpha-1,2-mannosidase IA) (Alpha-1,2-mannosidase IA) (P45700)
Organism: Mus musculus (Mouse)
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- alpha-1,2-Mannosidase
- Alpha-mannosidase 2
Sequence:
MPVGGLLPLFSSPGGGGLGSGLGGGLGGGRKGSGPAAFRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSNPALQPPAEHKPGLGARAEDAAEGRVRHREEGAPGDPGAGLEDNLARIRENHERALREAKETLQKLPEEIQRDILLEKEKVAQDQLRDKDLFRGLPKVDFLPPVGVENREPADATIREKRAKIKEMMTHAWNNYKRYAWGLNELKPISKEGHSSSLFGNIKGATIVDALDTLFIMGMKTEFQEAKSWIKKYLDFNVNAEVSVFEVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHLSHLSGDPVFAEKVMKIRTVLNKLDKPEGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSGGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADGAPEARAQHYLELGAEIARTCHESYNRTYVKLGPEAFRFDGGVEAIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRTWAWEAVEALESHCRVNGGYSGLRDVYIARESYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNTEAHPFPILREQKKEIDGKEK
Protein: Exocyst subunit Exo70 family protein (Q7XYW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component EXO84C
- Exocyst complex component EXO84B
- Exocyst complex component SEC3B
- Exocyst complex component SEC5B
- Exocyst complex component SEC3A
- Exocyst complex component SEC10a
- Exocyst complex component EXO84A
Sequence:
MMAESTGVDRGIQSLIAARKSLKLSLEKSKAIGLALGKTGPRFDEIEQRLPLLEAAVRPIRADGEALKDVGGNINRAVGPAAAVLKVFDAVHGLEKSLLSDPKNDLSSYLSVLKRLEEALKFLGENCGLAIQWLEDIVEYLDDHHVADEKYLSNLKKSLRGLSEFHNDRGGGEEKERSQLRLDGGLRNAALDKLENEFRRLLKDNSVPLPMASPSSLGDQACIAPSQLPVTVIHKLQAILGRLRANNRLDKCISIYVEVRSLNVRASLQALDLDYLDISVSEFNDVQSIEGYIAQWGNHLEFAVKHLFEAEFKLCNDVFERLGLNVWMDCFSKIAAQAGMLAFLQFGKTVTDSKKDPIKLLKLLDIFTSLNKLRADFNRLFGGAACIEIQNFTRDLIKRIIDGAAEIFWELLVQVEIQKQTPPPSDGGVPRLVSFVTDYCNKLIGDKYKSTLTQVLLIHKSWRSERFQDNQLMVEVLRIIKAIEQNLDVWMKAYPDQTLAHFFGMNNHWHLYKNLKGTNIGDHLGDSWLKEHDQYKEYYATVFLRDSWGKLPSHLSREGLILFSGGHATARDLVKKRLKAFNDAFDEMYKKQASWVLPEKDLRDRVCQQIVQAIVPVYRSYMQNYGPLVEKDASSSKYVRYTVVALEKILSSLYMPKPMRYGSFKGTPPSEKFKNDVDLRRTTSAVV
Protein: Antimicrobial peptide aurelin (Q0MWV8)
Organism: Aurelia aurita (Moon jellyfish) (Medusa aurita)
Function: Antimicrobial peptide with modest activity. Active against the Gram-positive bacterium L.monocytogenes (MIC=22.64 ug/ml), B.megaterium (MIC=10 uM), B.mycoides, B.subtilis, M.luteus (MIC=40 uM), M.phlei, and S.aureus, and the Gram-negative bacterium E.coli (MIC=7.66 ug/ml) and P.aeruginosa. Shows moderate affinity to the negatively charged (POPC/DOPG 3:1) lipid vesicles. The peptide interacts with the surface of DPC micelles by two alpha-helical regions. It does not interact with the zwitterionic (POPC) lipid vesicles, which model membranes of eukaryotic cells.
Subcellular location: Secreted {ECO:0000305}. Target cell membrane {ECO:0000269|PubMed:16890198, ECO:0000269|PubMed:23137541}. Note=Isolated from mesoglea. {ECO:0000305|PubMed:16890198}.
Interaction partners:
Sequence:
MGCFKVLVLFAAILCMSLLVCAEDEVNLQAQIEEGPMEAIRSRRAACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC
Protein: MTRF1L release factor glutamine methyltransferase (EC 2.1.1.297) (HemK methyltransferase family member 1) (Q921L7)
Organism: Mus musculus (Mouse)
Function: N5-glutamine methyltransferase responsible for the methylation of the glutamine residue in the universally conserved GGQ motif of the mitochondrial translation release factor MTRF1L.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y5R4}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Peptide chain release factor 1, mitochondrial
- Mitochondrial translation release factor in rescue
- Peptide chain release factor 1-like, mitochondrial
- Nicotinamide phosphoribosyltransferase
- F-box only protein 5
- Methyltransferase HEMK2
Sequence:
MKLWGQILWTLLSVPRGRRGVLQGWAFNSWKTYSSLTGPLSATGMVNHWTRVFEERGIPEARESSEYIVAHVLGAKTFQSLKPALWTKPLTPQQLECIQELCGRRLQRMPVQYILGEWDFQGLSLKMVPPVFIPRPETEELVEWVLEEVAQRPHAVRAQDGPLILEVGCGSGAITLSLLSQLPKSRVVAVDKEEAAVSLTHENAQRLQLQDRIRIIHLDITSEGCCTHLLPWSPLDLVVSNPPYIFRKDMEQLAPEICSYEDLVALDGGDEGMDIITHILTLAPQLLNASGSIFLEVDPRHPELVSSWLQSHPDLHLSLVGVREDFCGRPRFLHVQKSAP
Protein: Large ribosomal subunit protein uL18m (39S ribosomal protein L18, mitochondrial) (L18mt) (MRP-L18) (Q9H0U6)
Organism: Homo sapiens (Human)
Function: Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL38
- Large ribosomal subunit protein mL62
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein bL19m
Sequence:
MALRSRFWGLFSVCRNPGCRFAALSTSSEPAAKPEVDPVENEAVAPEFTNRNPRNLELLSVARKERGWRTVFPSREFWHRLRVIRTQHHVEALVEHQNGKVVVSASTREWAIKKHLYSTRNVVACESIGRVLAQRCLEAGINFMVYQPTPWEAASDSMKRLQSAMTEGGVVLREPQRIYE
Protein: Octopamine receptor beta-2R (CsOA2B2) (G3M4F8)
Organism: Chilo suppressalis (Asiatic rice borer moth)
Function: Autoreceptor for octopamine, which is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. Also acts as a receptor for tyramine, but with much less potency. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22786641}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPINGSHSGANATISDITNGAYNATDAGEWTSSVMFKLRTCVLLLIVIMAVLGNMLVIVSVMRHRKLRVITNYFVVSLAFADILVAMVVMPFNFSVQFNQGWVFGETICDLWNSSDVYFTSTSILHLCCISVDRYYAIVKPLKYPIKMTKKMAFVMLAATWLSPITISYVPIFMGWYTTTDFLESRRDDQCEFKVNKPYAVISSSISFWIPCTIMIFTYLAIFKEANRQEKALHARAGNAMLMHRHSREVSDKNGALHINATTPTKDRNLLKMKREHKAARTLGIIMGAFILCWLPFFLYYVSTSLCDSCNCPEVVTVIMFWTGYFNSALNPIIYAYFNRDFRNAFKNTLACAFCSFCKRSASDLDAMERLDRRGSAQLRVPIPSRRASDLASL
Protein: Signal transduction histidine-protein kinase AtoS (EC 2.7.13.3) (Q06067)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine. Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon. AtoS is a membrane-associated kinase that phosphorylates and activates AtoC in response to environmental signals.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16153782}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Regulatory protein AtoC
Sequence:
MHYMKWIYPRRLRNQMILMAILMVIVPTLTIGYIVETEGRSAVLSEKEKKLSAVVNLLNQALGDRYDLYIDLPREERIRALNAELAPITENITHAFPGIGAGYYNKMLDAIITYAPSALYQNNVGVTIAADHPGREVMRTNTPLVYSGRQVRGDILNSMLPIERNGEILGYIWANELTEDIRRQAWKMDVRIIIVLTAGLLISLLLIVLFSRRLSANIDIITDGLSTLAQNIPTRLPQLPGEMGQISQSVNNLAQALRETRTLNDLIIENAADGVIAIDRQGDVTTMNPAAEVITGYQRHELVGQPYSMLFDNTQFYSPVLDTLEHGTEHVALEISFPGRDRTIELSVTTSRIHNTHGEMIGALVIFSDLTARKETQRRMAQAERLATLGELMAGVAHEVRNPLTAIRGYVQILRQQTSDPIHQEYLSVVLKEIDSINKVIQQLLEFSRPRHSQWQQVSLNALVEETLVLVQTAGVQARVDFISELDNELSPINADRELLKQVLLNILINAVQAISARGKIRIQTWQYSDSQQAISIEDNGCGIDLSLQKKIFDPFFTTKASGTGLGLALSQRIINAHQGDIRVASLPGYGATFTLILPINPQGNQTV
Protein: Vegetative storage protein 1 (O49195)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as somatic storage protein during early seedling development.
Interaction partners:
- Defensin-like protein 16
- Lipoxygenase 2, chloroplastic
- Transcription factor MYC2
- Thionin-2.1
- Coronatine-insensitive protein 1
- Ethylene-responsive transcription factor ERF094
- Cystine lyase CORI3
- Cellulose synthase A catalytic subunit 3
- Protein TIFY 10A
- 12-oxophytodienoate reductase 3
Sequence:
MKILSLSLLLLLAATVSHVQSSASVPGLIELLESNTIFGNEAELLEKEGLSINYPNCRSWHLGVETSNIINFDTVPANCKAYVEDYLITSKQYQYDSKTVNKEAYFYAKGLALKNDTVNVWIFDLDDTLLSSIPYYAKYGYGTENTAPGAYWSWLESGESTPGLPETLHLYENLLELGIEPIIISDRWKKLSEVTVENLKAVGVTKWKHLILKPNGSKLTQVVYKSKVRNSLVKKGYNIVGNIGDQWADLVEDTPGRVFKLPNPLYYVPS
Protein: NAD-dependent histone deacetylase SIR2 (EC 2.3.1.286) (Regulatory protein SIR2) (Silent information regulator 2) (Q6FWI7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: NAD-dependent deacetylase. Heterochromatin component that silences transcription at silent mating loci, telomeres and the ribosomal DNA, and that also suppresses recombination in the rDNA and extends replicative life span. It acts as a NAD-dependent histone deacetylase, which deacetylates 'Lys-9' and 'Lys-14' of Histone H3 and 'Lys-16' of Histone H4 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Purine nucleoside phosphorylase
- NAD
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MIISRGSHVDEEPVAKKPRISVGEMTDDTTDDGLNTEEIRAPYTTEEMDEPEKAALLPKIPKKSPVSIGMNPENGKYVLPNYSKDESLNARKFLKYYGLRKFLDTYLPEELNSLYIYSLIKLLGFEIRDKELLSSLYRFFHPVKSSDQFKLEYEDFTDPLEKKEAVKLIKDLQKAINRVLATRIRLSNFYTIDHFVSKIKKAERILVLTGAGVSTSLGIPDFRSSEGFYSKIQHLGLDDPQDVFNYDIFMQDPSVFYNIAHMILPPENMYSPLHSFIKMLQDKGKLLRNYTQNIDNLESYAGIDPEKLVQCHGSFATASCVTCHWQIPGEKIFSNIRSMELPLCPYCYQKRREYFPNTGDEEYDTLKGNLESGIQNNNFALKSYGVLKPDITFFGEALPSKFHKTIREDIMKCDLLICIGTSLKVAPVSEIVNMIPAYVPQVLINKDPVKHAEFDIELLGFCDDVATVVAQKCEWDIPHKDWEGKLKKKRFDVNEIERGVFNIEAGSPE
Protein: EMSY transcriptional repressor, BRCA2 interacting (E9PMC9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPVVWPTLLDLSRDECKRILRKLELEAYAGVISALRAQGDLTKEKKDLLGELSKVLSISTERHRAEVRRAVNDERLTTIAHNMSGPNSSSEWSIEGRRLVPLMPRLVPQTAFTVTANAVANAAIQHNASLPVPAETGSKEVVVCYSYTSTTSTPTSTPVPSGSIATVKSPRPASPASNVVVLPSGSTVYVKSVSCSDEDEKPRKRRRTNSSSSSPVVLKEVPKAVVPVSKTITVPVSGSPKMSNIMQSIANSLPPHMSPVKITFTKPSTQTTNTTTQKVIIVTTSPSSTFVPNILSKSHNYAAVTKLVPTSVIASTTQKPPVVITASQSSLVSNSSSGSSSSTPSPIPNTVAVTAVVSSTPSVVMSTVAQGVKIITQQVQPSKILPKPVTATLPTSSNSPIMVVSSNGAIMTTKLVTTPTGTQATYTRPTVSPSIGRMAATPGAATYVKTTSGSIITVVPKSLATLGGKIISSNIVSGTTTKITTIPMTSKPNVIVVQKTTGKGTTIQGLPGKNVVTTLLNAGGEKTIQTVPTGAKPAILTATRPITKMIVTQPKGIGSTVQPAAKIIPTKIVYGQQGKTQVLIKPKPVTFQATVVSEQTRQLVTETLQQASRVAEAGNSSIQEGKEEPQNYTDSSSSSTESSQSSQDSQPVVHVIASRRQDWSEHEIAMETSPTIIYQDVSSESQSATSTIKALLELQQTTVKEKLESKPRQPTIDLSQMAVPIQMTQEKRHSPESPSIAVVESELVAEYITTVSHRSQPQQPSQPQRTLLQHVAQSQTATQTSVVVKSIPASSPGAITHIMQQALSSHTAFTKHSEELGTEEGEVEEMDTLDPQTGLFYRSALTQSQSAKQQKLSQPPLEQTQLQVKTLQCFQTKQKQTIHLQADQLQHKLPQMPQLSIRHQKLTPLQQEQAQPKPDVQHTQHPMVAKDRQLPTLMAQPPQTVVQVLAVKTTQQLPKLQQAPNQPKIYVQPQTPQSQMSLPASSEKQTASQVEQPIITQGSSVTKITFEGRQPPTVTKITGGSSVPKLTSPVTSISPIQASEKTAVSDILKMSLMEAQIDTNVEHMIVDPPKKALATSMLTGEAGSLPSTHMVVAGMANSTPQQQKCRESCSSPSTVGSSLTTRKIDPPAVPATGQFMRIQNVGQKKAEESPAEIIIQAIPQYAIPCHSSSNVVVEPSGLLELNNFTSQQLDDEETAMEQDIDSSTEDGTEPSPSQSSAERS
Protein: cyclin-dependent kinase (EC 2.7.11.22) (G5EAZ1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Cyclin dependent kinase inhibitor Pho81, putative
- Nucleoporin NSP1
- Protein kinase domain-containing protein
- Cyclin-dependent kinases regulatory subunit
- Cell division control protein
- M-phase inducer phosphatase
- G2/mitotic-specific cyclin
- G2/mitotic-specific cyclin-B
- Origin recognition complex subunit 2
- Glycerophosphocholine phosphodiesterase Gde1, putative
Sequence:
MTSQRPTSSSSSLLDIVANLASPKSLLFNAHHTNPPPSLPSQRAPTMDKSQQPSSFQQLEKLGEGTYATVFKGRNRQTGELVALKEIHLDSEEGTPSTAIREISLMKELKHESIVSLYDVIHTENKLMLVFEYMDKDLKKYMDTRGDRGQLDQATIKSFMHQLMSGIAFCHDNRVLHRDLKPQNLLINKKGQLKLGDFGLARAFGIPVNTFSNEVVTLWYRAPDVLLGSRTYNTSIDIWSAGCIMAELYTGRPLFPGTTNEDQLQKIFRLMGTPSERSWPGISQLPEYRANFHVYATQDLGLILPQIDPLGLDLLNRMLQLRPEMRIDAHGALQHPWFHDLPQLQAQLQQQQMAGYGGMMPPQQAY
Protein: 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) (Q9Y0F3)
Organism: Leishmania major
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361219}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361219}.
Interaction partners:
- Mevalonate kinase
- Farnesyl pyrophosphate synthase
- Squalene monooxygenase
- Hydroxymethylglutaryl-coenzyme A synthase N-terminal domain-containing protein
Sequence:
MRRSLLLACSAAKGESWASMSDTEIMKQVENKKIAFHGLEQALAPDYDRAIAIRREIVKKKICPSPAATHPLERVPYKNYDWSSVVGQSCENILGYVPVPVGLAGPLLLDGKEVALPMATTEGALVASAHRGARAINLSGGCRTAVLKEGMTRAPVVEVNSFDEAITVIKFCEERFDVLREAFESTTRFGKLLSIKCAMAGRQVHLRFSAFTGDAMGMNMITKGCDKALQVLQQHIPSVRVLTLSGNFCTDKKPSALNWVEGRGKSVVAEAVIKRDVVESVLKCTVDSVVSLNVTKNLRGSALAGSIGGFNAHAANIVAALYIATGQDPAQVVESATCMTTVDKAGEDLVISLMMPSIEVGAVGGGTGLSSQRAMLELMGCAGSNKEDPGAHSRQIARVVAGAVICGELSLLSGLAAGHLLSAHMKLNRKPPTP
Protein: pH-response regulator protein palA/rim20 (Q09807)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Vacuolar-sorting protein snf7
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting protein bro1
- Vacuolar protein-sorting-associated protein 25
- HAD-like hydrolase superfamily protein P8B7.31
Sequence:
MEFLNIPTKNTFHWSCDPLFNELKRLSCFKSFTYENDLKTFKALRSQLCLSHPSINSLSSFQTYHQLLCVLEQKHLSECVAPFVWTLSSSSNERESFENLIFEHACLIYRLACTYHTTAISLCNEKPPNLVQACQYFQLSAGCFRYINDFYIYTKSLDFNENLLKAWEIYCLAEAQTCIFSKANSNDTTSESIIVKILAKVFLLYEDAYKLFKNATGAPSIFVHWTYIQKLFYQTITYQIISRTSYSLNKYGENISYLRLSLLHCKEALKTRFDFGFNVKVYEKLEKLESSLQFELKRNERDNDFIHLQPEIPVGSFPLLDTVTMVQSITPDVLTDKTAAYPYFSTCLDKEFMDLIEEHEKNILDAAVKSIDCLTKEGTEKLFALMEEIKSVNDNRYITETSNKVMENFTEIKNLGGLEFLRSEASSLDCLIDKVNGTYRHCCQALDEIINSVKSSQNMKEKGFYSDVIKLHEEVSLLKVNVENSQNAKDTIQKDISAFGKDIFELSAQSERILSNLAEKKNPNTDQLLLQANSYLAQWDLLKDERNMLKKLGSNDYFNISMYSNHTDIHSLLKCFREAVDAKWNFRRQRERQEIIIQNVEKLKSYLNSFKVQAECSEISKILSFSQETEKKYKFLLQTVRNETEIARELYNIICRAEERYSQYENRYENENRLNKIKLQHSSSNAFNPEIHKIKFKSSKK
Protein: Casein kinase 1-like protein 9 (EC 2.7.11.1) (Dual specificity kinase 1) (Protein CASEIN KINASE I-LIKE 9) (Protein CASEIN KINASE I-LIKE 9 ALPHA) (Protein CASEIN KINASE I-LIKE 9 BETA) (Q9ZWB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate casein on serine and threonine residues, and poly(Glu,Tyr) in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16126836}. Nucleus {ECO:0000269|PubMed:16126836}.
Interaction partners:
- At3g49990
- Cytochrome P450, family 715, subfamily A, polypeptide 1
- Bystin
- Serine/threonine-protein kinase RIO2
Sequence:
MDLVIGGKFKLGRKIGSGSFGELYLGINVQTGEEVAVKLESVKTKHPQLHYESKLYMLLQGGTGVPNLKWYGVEGDYNVMVIDLLGPSLEDLFNYCNRKLSLKTVLMLADQLINRVEFMHTRGFLHRDIKPDNFLMGLGRKANQVYIIDFGLGKKYRDLQTHRHIPYRENKNLTGTARYASVNTHLGVEQSRRDDLEALGYVLMYFLKGSLPWQGLKAGTKKQKYDRISEKKVATPIEVLCKNQPSEFVSYFRYCRSLRFDDKPDYSYLKRLFRDLFIREGYQFDYVFDWTVLKYPQIGSSSGSSSRTRNHTTANPGLTAGASLEKQERIAGKETRENRFSGAVEAFSRRHPATSTTRDRSASRNSVDGPLSKHPPGDSERPRSSSRYGSSSRRAIPSSSRPSSAGGPSDSRSSSRLVTSTGGVGTVSNRASTSQRIQAGNESRTSSFSRAARNTREDPLRRSLELLTLRK
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1) (Trophoblast antigen FDO161G) (P14060)
Organism: Homo sapiens (Human)
Function: A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. Specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Also converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone. Expected to use NAD(+) as preferred electron donor for the 3beta-hydroxy-steroid dehydrogenase activity and NADPH for the 3-ketosteroid reductase activity (Probable).
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Aromatase
- Cytochrome P450 11B1, mitochondrial
- 17-beta-hydroxysteroid dehydrogenase type 3
- Steroid 21-hydroxylase
- Cytochrome P450 11B2, mitochondrial
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aldo-keto reductase family 1 member C3
- Cytochrome P450 7B1
Sequence:
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q580P7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MESRSDTKGTSHIAVAAAVPVLFMTLMRCGMAQTITEPSSDKVTNLCTEAKYTAHLADHIVAAAEEPEREISDMQIYAEAWNLLAASTNQTDKRAATYALAAYMSAAAAKAKQLQNGKYKAAVLAATYLQRRSALTRTLQAMRVKGKTAVGQFTKKQGEEASCSHKETPTLSDEGDCGRQDNAINHPESIAIDLRTATHIKLVHGSKLRPLELTHEADVRETTPSEQAQVKATGCKAVLRSDFYVTFIASTTKKEDKTGVTAIKIFAGDDANTSCAELKDATKKSEKDNDLLINKICTYITKPDPQIITISSLTPAMLANTTAVQVAFRSFVHAATGKAPSDAEIEMQLQKLYGGDKQHFKRDFVTILTTKNMTYHTGSGFVTETFLDAAKNNHAHKVLIYLKGQRAAAQAKQPRTNESEINGPVCGGEGQEECKLDEKKDPEKPNGTQMRKWPKALQWMITRQGGNCKTIQQEDCKEDCTWDEGACDGAVGISASMNISLFMAFLLLA
Protein: Copine-F (Q1ZXB3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MAETIRPISKIELRFKLADIKKPSSQIIVYCNSGDSKRFDLIGATERIDNKSEPFFNTTINIDYYFESVQKLYLLAINHNLKTLDFTKIDQLDVVGEFTPTIGDLISRDGKRLIGDIKDKDKITGKIEITAEEIYETGHNIILQLKGTKLDKKDLFSSDPYFKIYKSSPSGNSIVFESSVIKNNINPIFDPIVIRLQELNGGCMFRELTFEFWDHNDIVDDELIGSFRTNTDEILSGIIKEFPIINQKLKSKKSNYEHSGIINFIDSRILYKPTIQDFINGNGNGNGNGDGNCLIDLMVAIDCTESNGDQKLETSLHYNVKPHQNQYIRSLLALESQLLNNFGVKLEKRVEVFGFGAVINKHPNHNFRFHYIIDDRPNTLKAGISGVIELYDKAIPKIQFTSPTKISSIIEDATRYSLQDFHSTQLKYSILLILIDSDITDYESTVDEIVEASKAPLSIIFIGVGEYSFQNIPQLDGEKNGNIRLIGRFDRKQIRDNVHFISFKEFSINQIDFQNEILRKLPNQLTEFMEFKNYLPNGLSYTQTEIKKIK
Protein: DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan) (G3X912)
Organism: Mus musculus (Mouse)
Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}.
Interaction partners:
- Proliferating cell nuclear antigen
- Transitional endoplasmic reticulum ATPase
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Transmembrane phosphatase with tensin homology
- 3222402P14Rik protein
- DNA polymerase eta
- Tyrosyl-DNA phosphodiesterase 1
- Ubiquitin recognition factor in ER-associated degradation protein 1
Sequence:
MDEDLVVALRLQEEWDVQMARRAAAAREPVSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRQPYYGYVKRATNRAPSVHDYWWADHQKTCGGTYIKIKEPENYSKKGRGKTKADKQPASAVENKDKLCRGEAQLLIPFSGKGYVLGDASTCPSAGKLNTSYMVNEAKGLSSQDHSVSGLRLNSNAEVKCEQNCLPKKPHLVSPLPTASHQSVLSSYFPRVSVANQKAFRNVNGSPVKNGTTGDGTKRPASGGSQRKVPPSRASLRNTSKVTAPASATVTSAAGTSATISREESGSEDQFLNKRPRLEDRTALDTIKEQTQSGGDLRSSSQPTAASAPQSLSSQRRLVNCPVCQGVVVESQINEHLDRCLEGNKTNLRPRRV