wanglab/gogpt-training-data huggingface dataset:
Protein: APC/C activator protein CDH1 (CDC20 homolog 1) (Homolog of CDC twenty 1) (P53197)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). During telophase and in the subsequent G1 phase of the cell cycle, recognizes and binds proteins containing a destruction box (D-box) and an additional degradation signal termed the KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1. Probably is the target of a BUB2-dependent spindle checkpoint pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12456658}. Nucleus {ECO:0000269|PubMed:12456658}. Note=Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5.
Interaction partners:
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit CDC23
- Mitotic spindle checkpoint component MAD2
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit CDC27
- Securin
- Anaphase-promoting complex subunit 4
- Spindle assembly checkpoint component MAD1
- S-phase entry cyclin-5
Sequence:
MSTNLNPFMNNTPSSSPLKGSESKRVSKRPISSSSSASLLSSPSRRSRPSTVYGDRYIPSRTDIDFNSIVSISSMASVPALNPSSTEDQVEYQKERQAHETYNTLLKNELFGEMLSKDTVGSESSIDRIKNTRPSTRGNVHAENTTRHGYELERVSTPPPEAAGLEEFSPHSTPVTPRRLFTSQQDEITRPSSNSVRGASLLTYQQRKGRRLSAASLLQSQFFDSMSPVRPDSKQLLLSPGKQFRQIAKVPYRVLDAPSLADDFYYSLIDWSSTDVLAVALGKSIFLTDNNTGDVVHLCDTENEYTSLSWIGAGSHLAVGQANGLVEIYDVMKRKCIRTLSGHIDRVACLSWNNHVLTSGSRDHRILHRDVRMPDPFFETIESHTQEVCGLKWNVADNKLASGGNDNVVHVYEGTSKSPILTFDEHKAAVKAMAWSPHKRGVLATGGGTADRRLKIWNVNTSIKMSDIDSGSQICNMVWSKNTNELVTSHGYSKYNLTLWDCNSMDPIAILKGHSFRVLHLTLSNDGTTVVSGAGDETLRYWKLFDKPKAKVQPNSLIFDAFNQIR
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein (Cnt-b) (Centaurin-beta) (Q8C8T5)
Organism: Mus musculus (Mouse)
Subcellular location: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}.
Interaction partners:
Sequence:
SSDVLAFGTGSVVDSVTEEEGAESEESSSEVDGEAEAWSLADVRELHPGLLAHQAARTRDLPALAAALAHGAEVNWADAADEGKTPLVQAVLGGSLIVCEFLLQNGADVNQRDSLGRAPLHHATLLGRTGQVCLFLKRGADQHALDQEQQDPLTIAVQAANADIVTLLRLARMAEEMREAEAPPGQPGPLPGSSPTELQYRRCIQEFIGLHLEES
Protein: Aprataxin and PNK-like factor (EC 3.1.-.-) (Apurinic-apyrimidinic endonuclease APLF) (Q9D842)
Organism: Mus musculus (Mouse)
Function: Histone chaperone involved in single-strand and double-strand DNA break repair (By similarity). Recruited to sites of DNA damage through interaction with branched poly-ADP-ribose chains, a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (By similarity). Following recruitment to DNA damage sites, acts as a histone chaperone that mediates histone eviction during DNA repair and promotes recruitment of histone variant MACROH2A1. Also has a nuclease activity: displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro (By similarity). Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (By similarity). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Also acts as a negative regulator of cell pluripotency by promoting histone exchange. Required for the embryo implantation during the epithelial to mesenchymal transition in females.
Subcellular location: Nucleus {ECO:0000269|PubMed:33277378}. Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol {ECO:0000269|PubMed:33277378}. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}.
Interaction partners:
- DNA repair protein XRCC1
- DNA repair protein XRCC4
- X-ray repair cross-complementing protein 5
- Aprataxin
- X-ray repair cross-complementing protein 6
- Protein mono-ADP-ribosyltransferase PARP3
- Bifunctional polynucleotide phosphatase/kinase
- DNA polymerase beta
- DNA ligase 3
- DNA ligase 4
Sequence:
MPSDFFLQPLDGGPRVPVGPGQTVIGRGPLLGITDKRVSRRHAILEVVDSQLRIKPIHRNPCFYQSSEKSQHSPMETQVWSQLHPGDSFSLLLDKYAFRVFSAESEVEMECTLRNSQMLDEDDILSEMQKSPVVNLPDKTTGASQLQGSPEITKTKCPTIDPMSSSGECRAFSEHQPRPTQRKRILPAWMLAESLSDQSLSTPAEGGDKDVIQRSGKAGTCEDRTPGNTSWHGKKRLSPSGNSKSVSAEQDPGKKCRKADQEGPGVSSENVPESSSSNIVKDPDVDIVKTNKQKDGILIEELGEVSKHKAATKPTTNEEGESCARVQSKSPPEKSQGCHPESSSAPSSPDALHTDTADPVLGCSEESKVRRTACMYGANCYRRNPLHFQHFSHPGDSDYGEVHGTDEGVIGDRPECPYGASCYRKNPQHKMEYRHSALPARVALDEDDDDVGQPSDDEDEEDYEPTDEDSDWHPGKDDEEQEDVDELLKEAKSSLHLKH
Protein: Basic-leucine zipper (BZIP) transcription factor family protein (Putative VSF-1-like b-ZIP transcription factor) (Q9SKF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein At4g06598
- Sequence-specific DNA binding transcription factor
- Basic-leucine zipper
- Activator of spomin LUC3
- At5g04840
Sequence:
MNGSDNTTPSRPWSITQPSLAFSSLPPLSPSPSSSRRNSLPLMNPSTSMESRDSSMRFKKNSLLPPLGVKKIAPKDIGPLKRHYRSVSMDSCLSDLLKLTPSPGNTPSSRLVDGDQNASRLEFDANDYTDDELNKIAKSNKLKEVALDPKEVRRILKNRESAAHLKQKKLQYMINLEHRINFVENENASIFEKIKLLENDKTMMMNEKKEIMIRIESMEIQAQLRDVLTEHLHGESERLKAALISNENGNGKVQKLRMATCEVLQNRHEFDKSNMEVMDSNMINWSQPNPGFNG
Protein: L-talarate/galactarate dehydratase (TalrD/GalrD) (EC 4.2.1.156) (EC 4.2.1.42) (StTGD) (Q8ZL58)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the efficient dehydration of both L-talarate (also called L-altrarate) and galactarate to 5-keto-4-deoxy-D-glucarate (5-KDG). Also catalyzes the epimerization of L-talarate to galactarate; epimerization occurs in competition with dehydration. Is required for the utilization of L-talarate as a carbon source. Also functions in galactarate utilization. Is not active on other acid sugars.
Interaction partners:
- Glucarate dehydratase
- MFS family transport protein
- 5-keto-4-deoxy-D-glucarate aldolase
- Galactarate dehydratase
- 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase
- 3-oxo-tetronate 4-phosphate decarboxylase
- L-ribulose-5-phosphate 4-epimerase
- Permease
- Transcriptional regulator
Sequence:
MALSANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGRQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDIRRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
Protein: FabG-like protein (Hydroxysteroid (17-beta) dehydrogenase 8) (Q32S21)
Organism: Bos taurus (Bovine)
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Very-long-chain 3-oxoacyl-CoA reductase
- 17-beta hydroxysteroid dehydrogenase 2
- Hydroxysteroid
- Fatty acid synthase S-acetyltransferase; [Acyl-carrier-protein] S-malonyltransferase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl-[acyl-carrier-protein] reductase; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Enoyl-[acyl-carrier-protein] reductase; Acyl-[acyl-carrier-protein] hydrolase]
- 17beta-estradiol 17-dehydrogenase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase
- 17-alpha-hydroxyprogesterone aldolase
Sequence:
MASPLRLRSALALVTGAGGGIGRAISVRLAAEGAAVAACDLDGAAARETVQLLGGPGTEEGAPRGAHAAFQADVSEAGAARRLLEQVQACFSRPPSVVVSCAGITRDEFLLHMSEDNWDKVIAVNLKGIFLVTQAAAQALVSSGCPGSIINISSIIGKVGNMGQTNYAASKAGVIGLTQSAARELGRHGIRCNSVLPGFIRTPMTQKVPQKVLDKVTGMIPMAHMGNPEDVADVVAFLASEDSGYITGASVEVTGGLFM
Protein: Probable chromosome-partitioning protein ParB (Q9HT12)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Chromosome partitioning protein Soj
- AAA domain-containing protein
- Probable plasmid partitioning protein
- Ribosomal RNA small subunit methyltransferase G
- Radical SAM core domain-containing protein
- DNA translocase FtsK
- tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
- tRNA modification GTPase MnmE
- Ferredoxin
- Secreted protein
Sequence:
MAAKKRGLGRGLDALLGGSSPAKLQEEAVQADRRELQQIPLDLMQRGKYQPRRDMDPQALEELAQSIKAQGVMQPIVVRPIANGRYEIIAGERRWRASQQAGLEKIPALVRDVPDEAAIAMALIENIQREDLNPIEEAAALQRLQQEFQLTQQQVAEAVGKSRATITNLLRLIGLPEEIKTLLSHGDLEMGHARALLGLPAERQVEGARHVVAHGLTVRQTEALVRQWTHAPGKPAGPVKSDPDIARLEQRLAERLGASVQIRHGQKGKGQLVIRYSSLDELQGVLAHIR
Protein: Temporin-1Tk (TK) (Temporin-K) (P56923)
Organism: Rana temporaria (European common frog)
Function: Amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-positive bacteria, weak activity against Gram-negative bacteria, and moderate activity against fungi.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}.
Interaction partners:
Sequence:
LLPNLLKSLL
Protein: Gamma-soluble NSF attachment protein (Gamma-SNAP) (N-ethylmaleimide-sensitive factor attachment protein gamma) (Q9SPE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Binds to SNARE complex and then recruits NSF to disassemble it (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vesicle-fusing ATPase
- Alpha-soluble NSF attachment protein 2
- Alpha-soluble NSF attachment protein 1
- Syntaxin-42
- MAG2-interacting protein 2
- Putative syntaxin-24
- Golgi SNAP receptor complex member 1-1
- Golgi SNAP receptor complex member 1-2
- Syntaxin-31
- Syntaxin-32
Sequence:
MSSDPDKMMSKADKMTKLTLTRWSADWRGATELYEQAANGFRASNKYEKAKVALEKASKGQEMQASPWDAAKHMESAAALAQKLSIWNEVADFYRKASELYVECGRAQPASDALGKAARALEDVKPDDAIQLYTDACEILEEDGRDQMAFDLYRACANVYIKLEKFTDAATFFLRLGVAADKCDATNSQCKAYLSAIILYLYAHDLQQAEKCYNDCSQIDAFLKSDQSRSASRLLTAYNEGDIEEIKKVASASTVSNLDHMIIKLARKLPTGDVTAIQMNTNDDLDEDDLT
Protein: Substance-P receptor (NK-1 receptor) (Tachykinin receptor 1) (E9QCW0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Tachykinin 1
- Tachykinin receptor 1b
- Preprotachykinin 2a
- Tachykinin precursor 3b.
Sequence:
MDSFITSTDFPSNWTVNSTAQNETEIYWNQFVQPVWRIVLWAVAYSTIVVVSVVGNITVIWIILAHKRMRTVTNYFLVNLAFAEASMSAFNTVINFVYSVHNEWYFGLYYCRFHNFFPIAAVFASIYSMTAIALDRYMAIIHPLQQRMSATQTKVVIGVIWILALLLAFPQYYYSDTDQLPGRVVCYIDWPEYTLLDFKTMYFVCVAVLIYFLPLLVMGCAYLVVGLTLWASEIPGDSSDRYQEQLTAKRKVVKMMIVVVCTFAVCWLPYHVYFLIHQFYPHLFEHTFIQQVYLTIMWLAMSSTMYNPIIYCCLNDRFRAGFKQAFRCCPCVPEGSYEGLELKSTRYLQTQTSLYRASRMETSVSCVMQPSEDGHKVTFGSVRGAAVKPAARSPSREFTSNGSSSRSISKTVSETSSFYSSNNLQE
Protein: Calponin-homology (CH) domain-containing protein (D0IMZ5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAQPKRLDQEEEVVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATKPIIMKPKVQATISNLDKILQVNDPREFDLKLSRDGFKPKVSIRDEDGQDIHLSLKKVEDKENAYKVKFTPTKIGFIHVDVAANDVHTFETQTIPEASVICQVVPIARLLDYNKTAKVGDDVKFAVVDAIEGPVEAIVVDPTGKEHRMVILDGTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRGKPKNSFKVWGRGIAPEGIRKNDVVGVHVESLDPEENIANANISLEVLKPSDGSHLPVSVGYNDESQSMDFEYSPKQAPDDLEVLVKVAGEVIESHKIHVAPESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPSKAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHIQDSPFVLRVTEPIEGLKPSATRVTGIDESKVYNVGEKIPFRVDTRLCGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAGVSVPGAPFSVKVKEPTDASKLKIFGPGVDGPVYSKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGEEISPIEINVKPNVDVSGIRVEGLENENLLIGSHLRPTINIGKLEPKSKGLQLIDEVNGKRYNVPMKINPDGTYSTDTPLMEVGEHKLQLLFDEIPVKEAVVEVIKGTDVNKCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGKDEQKEHVKGSPFKAVVDYKKDPSQITISGLDQPNYRLNQPINFVIDTSKTKDLPVKATVPSDFAQLQPVVSRSPSNPRHHNVRFVPSGKPNVSIPIEIIYDGLKIDEKLVKVLPEVEPQLIKILHDKKKDSLTTTPITTNASHEGHVPFDVRDCGNVKKIESRVFGPDGKERLNHVRSTEQNGIYDVSFPTDMAGEYCVVFYINGQEVAARVPVMAEKIGRKEDVIKEEIVFHPEIAEHSPTVLTYNHPIDAKKKKAHPAIQVLAAKPDAVRLEHIQELVDNGHRVADRIVFTATKLGTNTLDVFYGGEHVDHVEYEAIGKLEYERIQAERAKVVVEKEDDVDKYEKQYKDEPSSAPADPRVAPTNGKEPTTAQESKKNGNQQKLAPSAEIEHKPLEKYFTFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVDAYGDGWATVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPAKSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDSPFRVLVMGEGQKRSHLSVGSTSEVALPITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRDGKLVPKAPFKIKVDKTQVGDASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPSKAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHHVKDSPLTVQCTGKSAGRVIQTIQKDVEQHGICLPDQESHLFLKLLNTSPMDITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPFQFTVGSFSEGGAHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPSKATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQHIPDSPFKVYIAPATGEVRKLELAQFHGQGIPAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGESYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRVGGKDLCDPTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKGYKVRYTPLAPGSYFASVKYNGIHAPGSPFKIPVEGKELGGNGYNETSHVKIDAVAKTSKGTVAVVPEYQGDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKEIPGSPFAIEP
Protein: Intraflagellar transport protein 122 homolog (WD repeat-containing protein 10) (WD repeat-containing protein 140) (Q9HBG6)
Organism: Homo sapiens (Human)
Function: As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is required in ciliogenesis and ciliary protein trafficking. Involved in cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:29220510}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29220510}. Note=Localizes to photoreceptor connecting cilia. {ECO:0000250|UniProtKB:Q6NWV3}.
Interaction partners:
- WD repeat-containing protein 35
- Intraflagellar transport protein 43 homolog
- Tetratricopeptide repeat protein 21B
- Intraflagellar transport protein 140 homolog
- WD repeat-containing protein 19
- PTB domain-containing engulfment adapter protein 1
- Tubby-related protein 3
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport-associated protein
- Intraflagellar transport protein 172 homolog
Sequence:
MRAVLTWRDKAEHCINDIAFKPDGTQLILAAGSRLLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKLEGILKYTHNDAIQCVSYNPITHQLASCSSSDFGLWSPEQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKIERPGGSLSPIWSICWNPSSRWESFWMNRENEDAEDVIVNRYIQEIPSTLKSAVYSSQGSEAEEEEPEEEDDSPRDDNLEERNDILAVADWGQKVSFYQLSGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLFTKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLIFSTVHGLYKDRYAYRDSMTDVIVQHLITEQKVRIKCKELVKKIAIYRNRLAIQLPEKILIYELYSEDLSDMHYRVKEKIIKKFECNLLVVCANHIILCQEKRLQCLSFSGVKEREWQMESLIRYIKVIGGPPGREGLLVGLKNGQILKIFVDNLFAIVLLKQATAVRCLDMSASRKKLAVVDENDTCLVYDIDTKELLFQEPNANSVAWNTQCEDMLCFSGGGYLNIKASTFPVHRQKLQGFVVGYNGSKIFCLHVFSISAVEVPQSAPMYQYLDRKLFKEAYQIACLGVTDTDWRELAMEALEGLDFETAKKAFIRVQDLRYLELISSIEERKKRGETNNDLFLADVFSYQGKFHEAAKLYKRSGHENLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADWARNIKEPKAAVEMYISAGEHVKAIEICGDHGWVDMLIDIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQWLAENDRFEEAQKAFHKAGRQREAVQVLEQLTNNAVAESRFNDAAYYYWMLSMQCLDIAQDPAQKDTMLGKFYHFQRLAELYHGYHAIHRHTEDPFSVHRPETLFNISRFLLHSLPKDTPSGISKVKILFTLAKQSKALGAYRLARHAYDKLRGLYIPARFQKSIELGTLTIRAKPFHDSEELVPLCYRCSTNNPLLNNLGNVCINCRQPFIFSASSYDVLHLVEFYLEEGITDEEAISLIDLEVLRPKRDDRQLEIANNSSQILRLVETKDSIGDEDPFTAKLSFEQGGSEFVPVVVSRLVLRSMSRRDVLIKRWPPPLRWQYFRSLLPDASITMCPSCFQMFHSEDYELLVLQHGCCPYCRRCKDDPGP
Protein: Phosphoglucosamine mutase (EC 5.4.2.10) (P31120)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate.
Interaction partners:
- Bifunctional protein GlmU
- Glutamine--fructose-6-phosphate aminotransferase
- Dihydropteroate synthase
- N-acetylglucosamine-6-phosphate deacetylase
- Glucosamine-6-phosphate deaminase
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- ATP-dependent zinc metalloprotease FtsH
- Phosphoglucomutase
- Protein RecA
Sequence:
MSNRKYFGTDGIRGRVGDAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCKATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAVTAEVEAALGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKAV
Protein: Uncharacterized protein (Q8C333)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKKKNKASFLQPHGHTLTGTHTHTHTDAHAHTLALCPFGSSVLVFPSSIKLRYFRLRCIQYSPSSLSQVTVSGGSNLIPAQNLWEPFFNRELSSLVSDAAHSFKLVFISLWHGIFFFFFGPSHPGFLFGFSRKYLI
Protein: RRM domain-containing protein (D5MCQ1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKPMNPQ
Protein: Rac guanine nucleotide exchange factor B (Q55E26)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the regulation of the late steps of the endocytic pathway.
Subcellular location: Late endosome {ECO:0000269|PubMed:16781009}.
Interaction partners:
- EF-hand domain-containing protein
- Epidermal growth factor receptor substrate 15 homolog
- AP-1 complex subunit beta
- AP-4 complex subunit beta
- phosphoinositide 5-phosphatase
- SH3 and F-BAR domain-containing protein DDB_G0274695
- AP-2 complex subunit mu
- Rho-related protein racB
- Rho-related protein racC
- NECAP PHear domain-containing protein
Sequence:
MFSNFFGSSKRNTIASSSSSSKKDKDNGKDESSKLKNSGSSTLPKPITNNESGNNFITSPSVSSPLISPLSSSPSPLLSSSSNSIQSTSHQQQQQHQGVITSLQMKPSCTSLTDDIEKKKQAKYDSSLEQTARKWVCDVLEIQLEDDKTFYELFKNGVLLCRLINKLRGGTIKRINESTISFKQLENIENYLKACKTLGLQSVNLFNSIDLHENKDISLVITNIVVLGKHASKIEGYNGIHLAGERKIIKITTTPVSPLFGGNHNNNNNNNNNNNTSNGDLSPVSITSASGGSSNYNSYSNNPLNKSSNGKKAKWRKSVKIPAVSSLNSDIRTKEAFKFSPELQKAAQDWIEEVTKEKFKLPSFSSSLKDGILLCRVINTIIPNTILYINNGNSSFKKMENIGNYLKGCLVVGLKKTDLFDTPDLFEEKNINFVISNIHVLGNHVNKMYSHLKLPLIKNIGNGGNGGNGGIGGGGGSDGSPLKMYSSIIHSKFGNGSSNTSSGNGGVIIPPEDMKDLKDWINHHLRAHHSLQIGSDMSNDLRNGVTLLTLLEELTLQKVGIFAREPVLPWHFMQNICLLLNFLRENSVHNVSDISPHDLFNGDIHSLCMITRLIRENFDTDHQMKSIPMDTRRQKVIEEIIATEQSYVKSLSTVYNLLIVPLLNSLDTNSPILSNDEISSIFGNWEHLLRSHINLLKEFKLKLNLPFNDLTIDDSNQNQNHNNIFGDSIFDSNITIGDVFLEKCEFLKDNYTNYINNYDNSYQRVKRLKKSNSNFEELVNTFEIFQDTHNGLDLYSYLIMPIQRIVRYILLLKEVIKYTPSTHPDYQMLQNAKENIKRVADHVNESKMAVENKRKILSIQDSIQNLQFNLMDKERTYIREGFLEIEDTFKKDSYFFLFSDLLLFVKYKPSEETGKEFKYKEVFYLDQVVDVSDILSDDEGEACVDGDDDGGEYEGGNGDATSGSADPEDQTLRRSCNSNNNNNSNSNKSNTVYSFEIETCEFSLVLLAESHTEKIEWMEDLRSCLQHQLIKEEDQLSSLSLSDNDDDNDADADVESSLNSISSPLLLLNNNNIINNNNNNNNNNNNNNNNNNNNNNCKNSNININSSIDNNSDNNNNDYDSKINSEENGDSSDEENKTSNRRSVSFKTHKRLESDETISDTESDDYELVCGRSKKSQPPPVPPRKITFSDTIKNIDNQ
Protein: Acyltransferase helD2 (EC 2.3.1.-) (Helvolic acid biosynthesis cluster protein D2) (Q4WR23)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Cytochrome P450 monooxygenase helB1
- Cytochrome P450 monooxygenase helB4
- Cytochrome P450 monooxygenase helB2
- 3-ketosteroid 1-dehydrogenase helE
Sequence:
MEGLNISNQVFDLSPLDIIPSHLYITNAFFYENKTPGPRPFMQSSLLKESLYRALQNFPILLGHVRRHRRNAMQIVVDCDNLNLPLYEEQTHPQLHFRHLKDHQFHRDVWPKDANIIDPRASPNGELLQVHVHRLAEESGVVMVVRIAHCAVDAKGFVDFMQSWGWFARNHSHPEGDSWPRLLADRRVMYEYLPPDVQPAAPRSMWHPASWLLGLLSTLVVLFLGLYKRLLGDKTPPDEIESHLFSVPPHTLDRLRYTATCIDPSSRVSDHDIITALFTLAFAHTKHLLTCRTQTVTAIVPCDFRHRIGVPSNFTGSCAIGLYVSIPGSLLQTPLTAESVARAALLSRAVVDTADKVTIQTFIRRALRAIAFVGDKVNVLYATMVSQAFSNQSRLGFYEVDFGAGGPVMVAPMAYSNTVAVICPAPGPGGDGVGVRVFLTLRPEVMRMLLAKGFLDEFTDMIY
Protein: Thymosin beta-4 (T beta-4) (Fx) [Cleaved into: Hemoregulatory peptide AcSDKP (Ac-Ser-Asp-Lys-Pro) (N-acetyl-SDKP) (AcSDKP) (Seraspenide)] (P62328)
Organism: Homo sapiens (Human)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:1999398}.
Interaction partners:
- LIM and senescent cell antigen-like-containing domain protein 1
- Actin, cytoplasmic 2
- Scaffold protein ILK
- Actin, cytoplasmic 1
- Profilin-1
- Profilin-3
- Profilin-4
- Thymosin beta-4, Y-chromosomal
- Gelsolin
- Cofilin-1
Sequence:
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Protein: Zinc finger protein 496 (NSD1-interacting zinc finger protein 1) (Zinc finger protein with KRAB and SCAN domains 17) (Q5SXI5)
Organism: Mus musculus (Mouse)
Function: DNA-binding transcription factor that can both act as an activator and a repressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
Sequence:
MPTALCPRVLAPKESEEPRKMRSPPGENPSPQGEPPSPESSRRLFRRFRYQEAAGPREALQRLWELCRGWLRLERHTKEQILELLVLEQFLAILPWEIQSWVRAQEPESGEQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGDGPAAPQDLEQERMSAESQSYPDAPPGALVQGTGLLSRSPGQPSEDLVPQDAFVVQEQSIRDAQPVATCQLPPNRVSPFKDMILCFSEEDWSLLDPAQTGFYGEFIIGEDYAVSMPPNEPPVQPGHSHEEENGLRVTEWTTDLQDKEIPQASCLDLSSLQPFQGEERRKWEELQVPELQPCPQVVLSQSPCPAGGDPPALKSSLDQEVTIEIVLSSSGDEDSQHSPYCTEELRSPPEDLHSVPAHQSNASAEGEVQTSQKSYVCPNCGKIFRWRVNFIRHLRSRREQKPHKCSVCGELFSDSEDLDGHLETHEAQKPYRCTACGKSFRLNSHLISHRRIHLQPASQQPMKKSEEEALETEGTGASDLLEKSKAKLSFQCGDCEKSFQRHDHLVRHRRHCHLKDETRPFQCRYCVKTFRQNYDLLRHERLHMKRRSKQALNSY