wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-galactosidase 9 (Lactase 9) (EC 3.2.1.23) (Q9SCV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Protein IQ-DOMAIN 9
Sequence:
MAESIRTFSLQWRILSLIIALLVYFPILSGSYFKPFNVSYDHRALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIGSSGLYLHLRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMREAKLFCWQGGPIIMLQIENEYGDVEKSYGQKGKDYVKWAASMALGLGAGVPWVMCKQTDAPENIIDACNGYYCDGFKPNSRTKPVLWTEDWDGWYTKWGGSLPHRPAEDLAFAVARFYQRGGSFQNYYMYFGGTNFGRTSGGPFYITSYDYDAPLDEYGLRSEPKWGHLKDLHAAIKLCEPALVAADAPQYRKLGSKQEAHIYHGDGETGGKVCAAFLANIDEHKSAHVKFNGQSYTLPPWSVSILPDCRHVAFNTAKVGAQTSVKTVESARPSLGSMSILQKVVRQDNVSYISKSWMALKEPIGIWGENNFTFQGLLEHLNVTKDRSDYLWHKTRISVSEDDISFWKKNGPNSTVSIDSMRDVLRVFVNKQLAGSIVGHWVKAVQPVRFIQGNNDLLLLTQTVGLQNYGAFLEKDGAGFRGKAKLTGFKNGDLDLSKSSWTYQVGLKGEADKIYTVEHNEKAEWSTLETDASPSIFMWYKTYFDPPAGTDPVVLNLESMGRGQAWVNGQHIGRYWNIISQKDGCDRTCDYRGAYNSDKCTTNCGKPTQTRYHVPRSWLKPSSNLLVLFEETGGNPFKISVKTVTAGILCGQVSESHYPPLRKWSTPDYINGTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSGTLKTLAVMSRCSPSQNMSDLSF
Protein: PAP-associated domain-containing protein (O44768)
Organism: Caenorhabditis elegans
Interaction partners:
- Exonuclease mut-7
- MUTator
- MUTator
- RNA helicase
- RNase NYN domain-containing protein
- RNA-directed RNA polymerase
- SH2 domain-containing protein
- Argonaute protein hrde-1
- DRBM domain-containing protein
- Piwi-like protein ergo-1
Sequence:
MSQPNKDQRSPEDIDFKVKANPKAFHKFNGKFQRVLRDHEDDFNILSISMQDHFDTTKQPKEEFGKKMDWCYQLKNIISKNNPTWLFNIVPTGSTVTGLATKNSDLDVAIHIPQAARVLEQEERGRNITDDERQASWREIQLEILQIVRLNLQNDEQINSRINWEHGIQLVQAQIQILKVMTVDGIDCDISVVMDRFLSSMHNSFLIRHLAHIDGRFAPLCAIVKQWAASTKVKDPKDGGFNSYALVLLVIHFLQCGTFPPILPNLQEIFKKDNFIAWDDKVYPSILNFGAPLPKPLPRIAPNNAPLARLFIEFLYYYSMFNFKENYIGARPVMVMDRRTSQNNMVRSSTNKEVCIQDPFDEHNPGRTVRTLNRIKDVMRSTYQKFLPVEGSEFTFPTLDDIINMSPEVPKPSRAEVRNFRAEATEVNRVGLGVYCRNSFV
Protein: Casein kinase 1-like protein 8 (EC 2.7.11.1) (Protein CASEIN KINASE I-LIKE 8) (Q9LSX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell junction, plasmodesma {ECO:0000269|PubMed:16126836}. Note=Present in punctate particles with granular structure. {ECO:0000269|PubMed:16126836}.
Interaction partners:
- At3g49990
- Bystin
- Serine/threonine-protein kinase RIO2
Sequence:
MDRVVGGKYKLGRKLGSGSFGELFLGVNVQTGEEVAVKLEPARARHPQLHYESKLYMLLQGGTGIPHLKWYGVEGEYNCMVIDLLGPSMEDLFNYCSRRFNLKTVLMLADQMINRVEYMHVRGFLHRDIKPDNFLMGLGRKANQVYIIDYGLAKKYRDLQTHRHIPYRENKNLTGTARYASVNTHLGIEQSRRDDLESLGYVLMYFLRGSLPWQGLRAGTKKQKYDKISEKKRLTPVEVLCKSFPPEFTSYFLYVRSLRFEDKPDYPYLKRLFRDLFIREGYQFDYVFDWTILKYPQFSSGSSSSSKPRSSLRPAMNPPVPIAERPDKPSAGAGQDSRDRFSGALEAYARRNGSGSGVVQADRSRPRTSENVLASSKDTTPQNYERVERPISSTRHASSSRKAVVSSVRATSSADFTENRSSRVVPSNGRSSTAQRTQLVPDPTTRPSSSSFTRAAPSRTARDITLQSFELLTIGNGKRK
Protein: Csp37p (Q5A9D4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Metalloaminopeptidase
- Asr2p
- Hsp12p
- Tfs1p
- Wh11p
- Meiotic sister chromatid recombination protein 1
- Glutathione S-transferase omega-like 2
Sequence:
MSAGKYLLGTAALVGGVYYYDQYVQPILPRQQHQELAYQTQRVENKGSELNNKLTKKIEEGKKFVNEKTESVTKQVKNSDVYQKLQSNTEDYKKHVEDAVDNDKNVFVVGIQKYIDFVNQLGEGKVQTGTTQYSTVSPNVEVKEKSIFGNWFDKSDNKVDQLKNDADKKINEAKDKAESTKSDFFNWNSKKADELDKKANEAINWTNKQIDYASAEWHKHYEQAKGDWNKALDDLSKQWNDSKKQLNGRFDTEKDRAIKGVEDAKSNFEKLSNDLANDASKNQKLKDAQDHFGKSLENLKLFGDDVYNDFAKRFDDLFNRK
Protein: Regucalcin (RC) (Gluconolactonase) (GNL) (EC 3.1.1.17) (Senescence marker protein 30) (SMP-30) (Q03336)
Organism: Rattus norvegicus (Rat)
Function: Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable gluconokinase
- L-gulonolactone oxidase
- Catalase
- Protein transport protein Sec16B
- Parkinson disease protein 7 homolog
- Sorbitol dehydrogenase
- Phenylalanine-4-hydroxylase
- Calmodulin-like protein 4
- Arylacetamide deacetylase
- Choline dehydrogenase, mitochondrial
Sequence:
MSSIKIECVLRENYRCGESPVWEEASKCLLFVDIPSKTVCRWDSISNRVQRVGVDAPVSSVALRQSGGYVATIGTKFCALNWEDQSVFILAMVDEDKKNNRFNDGKVDPAGRYFAGTMAEETAPAVLERHQGSLYSLFPDHSVKKYFDQVDISNGLDWSLDHKIFYYIDSLSYTVDAFDYDLPTGQISNRRTVYKMEKDEQIPDGMCIDVEGKLWVACYNGGRVIRLDPETGKRLQTVKLPVDKTTSCCFGGKDYSEMYVTCARDGMSAEGLLRQPDAGNIFKITGLGVKGIAPYSYAG
Protein: Protein crumbs homolog 2 (crumbs2) (Crumbs-like protein 2) (Q80YA8)
Organism: Mus musculus (Mouse)
Function: Apical polarity protein that plays a central role during the epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly specified mesodermal cells move inside the embryo. Acts by promoting cell ingression, the process by which cells leave the epithelial epiblast and move inside the embryo to form a new tissue layer. The anisotropic distribution of CRB2 and MYH10/myosin-IIB at cell edges define which cells will ingress: cells with high apical CRB2 are probably extruded from the epiblast by neighboring cells with high levels of apical MYH10/myosin-IIB. Also required for maintenance of the apical polarity complex during development of the cortex.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:17920587, ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:27870829}; Single-pass type I membrane protein {ECO:0000255}. Note=O-glucosylation is required for localization at the apical plasma membrane (PubMed:26496195). Distributed in a complex anisotropic pattern on apical cell edges: the level of CRB2 on a cell edge is inversely correlated with the level of MYH10/myosin-IIB (PubMed:27870829). {ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:27870829}.
Interaction partners:
- InaD-like protein
- Protein crumbs homolog 3
- Protein PALS1
- Multiple PDZ domain protein
- Protein crumbs homolog 1
- Carbonyl reductase 1])
Sequence:
MALVGPRIWGPRRDIYPLLLLLLLLLLLLLPWVPAGLVPPETPSVCASDPCAPGTKCQATESGGYTCEPSELGGCATQPCHHGALCVPQGPDPNSFRCYCVPGFQGPHCELDIDECASRPCQHGGTCQNLADHYECHCPLGYAGVTCEAEVDECSSAPCLHGGSCLDGVGSYRCVCAPGYAGANCQLDVDECQSQPCAHGGVCHDLVNGFRCDCADTGYEGARCEQEVLECASAPCAHNASCLDGFRSFRCLCWPGFSGERCEVDEDECASGPCQNGGQCLQRSDPTLYGGVQAIFPGAFSFSHAAGFLCSCPLGFAGNDCSMDVDECASGPCLNGGSCQDLPNGFQCYCQDGYTGLTCQEDMDECQSEPCLHGGTCSDTVAGYICQCPEAWGGHDCSVQLTGCQGHTCPLAATCIPTFKSGLHGYFCRCPPGTYGPFCGQNTTFSVVSGSSVWGLVPAAASLGLALRFRTTLLAGTLATLKDTRDSLELVLVGAVLQATLSRHGTAVLILTLPDLALNDGHWHQVEVTLHLGTLELRLWHEGCPGQLCVASGPVATGPTASVASGPPGSYSIYLGGGVFAGCFQDVRVEGHLLLPEELKGTVLLGCERREPCQPLPCAHGGACVDLWTHFRCDCPRPYRGATCTDEVPAATFGLGGATSSASFLLHQLGPNLTVSFFLRTREPAGLLLQFANDSVASLTVFLSEGQIRAEGLGHPAVVLPGRWDDGLPHLVMLSFGPDQLQDLGQRLYVGGRFYPDDTQLWGGPFRGCLQDLQLNSIHLPFFSSPMENSSWPSELEAGQSSNLTQGCVSEDTCNPNPCFNGGTCHVTWNDFYCTCSENFTGPTCAQQRWCPRQPCLPPATCEEVPDGFVCVAEATFREGPPAVFTGHNVSSSLSGLTLAFRTRDSEAGLLRAVSAAGAHSNIWLAVRNGSLAGDVAGSVLPAPGPRVADGAWHRVRLAREFPQAAASRWLLWLDGAATPVALHGLGGDLGFLQGPGAVPLLLAENFTGCLGRVALGDFPLPLAPPRSGTVSGAREHFVAWPGSPAVSLGCRGGPVCSPSPCLHGGACRDLFDAFACSCGPAWEGPRCEIRADPCRSTPCVRGQCHARPDGRFECRCPPGFSGPRCRLPVLPQGCNLNSTCKDGAPCEGGPLGTNCSCQEGLAGLRCQSLDKPCEASPCLNGGTCRVASGIFECTCSAGFSGQFCEVVKTLPLPLPFPLLEVAVPAACACLLLLLLGLLSGILAARKRRQSEGTYSPSQQEVAGARLEMDSVLKVPPEERLI
Protein: ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor) (Sigma-24) (P0AGB6)
Organism: Escherichia coli (strain K12)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane. Indirectly activates transcription of csrB and csrC, 2 sRNAs that antagonize translational regulator CsrA, linking envelope stress, the stringent response and the catabolite repression systems.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522}. Note=Associates with the inner membrane via RseA (PubMed:11777003, PubMed:9159522). {ECO:0000269|PubMed:11777003}.
Interaction partners:
- Anti-sigma-E factor RseA
- Sigma-E factor regulatory protein RseB
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- Protein RseC
- RNA polymerase sigma factor RpoD
- RNA polymerase sigma factor FliA
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor RpoS
Sequence:
MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQEAFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR
Protein: Protein MODIFYING WALL LIGNIN-2 (MWL-2) (O65708)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with MWL1, contributes to secondary cell wall biology, specifically lignin biosynthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26930070}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- At1g52910
- Protein DESIGUAL 2
- At4g27438
- Transmembrane protein
- Probable LRR receptor-like serine/threonine-protein kinase At1g07560
- WAT1-related protein At4g01430
- Cysteine-rich repeat secretory protein 55
- Glutathione S-transferase L1
- 7-dehydrocholesterol reductase-like protein
- Cysteine-rich receptor-like protein kinase 19
Sequence:
MHNLFLYSVVFSLGLVSFITCFAAEFKRTQKEDIRWDTERNCYVPGSHAFGLGSAAVLCFCLAQIVGNIVVFRNHRTRTKREDGYKITDLTLPTVLLLLSWSNFVVVVLILSTAISMSRAQAYGEGWLDEDCYLVKDGVFAASGCLAILGLGALTISATRIKVKKQQQLVQVVIKDQNQDQRRSMEEEQKHDEHQTNKSESVIHLVEEVSSTNISRI
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (EC 3.6.4.12) (ATP-dependent helicase SMARCAD1) (Enhancer trap locus homolog 1) (Etl-1) (Q04692)
Organism: Mus musculus (Mouse)
Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:8219362}. Chromosome {ECO:0000250}. Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity). {ECO:0000250}.
Interaction partners:
- Transcription intermediary factor 1-beta
- Exonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA mismatch repair protein Msh2
- E3 ubiquitin-protein ligase TRIM33
Sequence:
MNLFNLDRFRFEKRSKIEEAPEAAPQPSQARPSSPISLSAEEENAEGEGSRANTPDSDVTEKTEDSSVPEPPDNERKASLSCFQNQRAIQEYIDLSSDTEDVSPNCSSTVQEKKFSKDTVIIVSEPSEDEESHDLPSVTRRNDSSELEDLSELEDLKDAKLQTLKELFPQRSDSDLLKLIESTSTMDGAIAAALLMFGDAGGGPRKRKLSSSSEEDDVNDDQSVKQPRGDRGEESNESAEASSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDVQCASQSEVTNGKEVARNQNYSKNATKIKMKQKISVKPQNGFNKKRKKNVFNPKKAVEDSEYDSGSDAGSSLDEDYSSCEEVMEDGYKGKILHFLQVSSIAELTLIPKCSQKKAQKITELRPFNNWEALFTKMSKINGLSEDLIWNCKTVIQERDVVIRLMNKCEDISNKLTKQVTMLTGNGGGWNREQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQYYTPEKLKEMSQLMLKEPTHCEANPDLIFEDMEVMTDFELHVLCKQYQHINSYQLDMDLILDSGKFRALGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLEQDMTTVDEADEGSMPADIATLLKTSMGL
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (Q8I7C6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATP-dependent DNA helicase ku70
- X-ray repair cross-complementing protein 5
- poly
- DNA cross-link repair 1 protein
- DNA-dependent protein kinase catalytic subunit
Sequence:
MPPKKRQLSQSDEDVKTTTTTTTSTSTKPLTEIFDGIVFCFSGTFSVTQTELTKKVEGCGASTSKTCTAKVTHLVSTVDDFKKNGTAVSKALKSGIPIVTEGFITKSIEASKKLEEKDYSLSSSNDDEEEEEEEEEEEEEEEEEEVAKPTRRSSKKAPAKSEEKGEDKNKLTTRPTKKTKTNTSEAETKTAASDLDDSSSESEDEKNQISVKIKGRAANDPHFPDSRFHVYENGKDVYDATLNQTEISQNNNKFYIIQLLEADDGSSYSVWNRWGREGLKGQSSRKDFGKGGLNQAISLFCSKFYEKTKNTFTDRANFKKVAGKYDMIELDYSTDSKPKNGASTTATTTTTKKVVEHKKECSLDERVQELVKLIFDVKMMERTMTEAKYDLKKMPLGKLSKNQITKGYLVLKQIEDVMGGKSGESLSTLSSRFYTIIPHAFGMSVPPVINTNQMLIEKMNMLQNLADIEIATNIIKDSESDESNILELHYAKLKTDIQPLDENSCEYKNILLYVKNTYQGGKKPTIVNIFKIDRDGEADRYKTKKHLGNRKLLWHGSRLTNYASIISQGLRIAPPEAPVSGYRFGKGVYFADCMSLSANYCRTVGSNDFCMLLGDVALGKTADLARDTYMEKPQPNSHSTWALGTVEPDPKVFFQDTEGCITPYGQMIPSQHKGVSCYEHQYVVYDVAQVHLKYLLQLRN
Protein: Actin nucleation-promoting factor WAS (Wiskott-Aldrich syndrome protein) (WASp) (P42768)
Organism: Homo sapiens (Human)
Function: Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. Promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8625410}. Nucleus {ECO:0000269|PubMed:20574068, ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2
- WAS/WASL-interacting protein family member 1
- SH2/SH3 adapter protein NCK1
- Hematopoietic lineage cell-specific protein
- Cell division control protein 42 homolog
- Cdc42-interacting protein 4
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- Src substrate cortactin
Sequence:
MSGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD
Protein: Acetylpolyamine amidohydrolase 1 (APAH 1) (EC 3.5.1.-) (Acetylcadaverine deacetylase) (Acetylpolyamine deacetylase) (Acetylputrescine deacetylase) (EC 3.5.1.62) (Q9I3T5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N(1)-acetylspermine and N(1)-acetylspermidine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. In vitro, can also hydrolyze artificial trifluoroacetylated and acetylated lysine-derivatives.
Interaction partners:
- Probable periplasmic spermidine/putrescine-binding protein
- Bis
- Probable AMP-binding enzyme
- Tryptophan 2-monooxygenase
- Uncharacterized protein
Sequence:
MLSVYSDDHRLHFGQSELVDGKLQPCFEMPSRADTVLARVKSQNLGEVIAPKDFGREPLLRLHDAAYLDFLQGAWARWTAEGHSGDLVSTTFPGRRLRRDGPIPTALMGELGYYSFDTEAPITAGTWQAIYSSAQVALTAQEHMRQGARSAFALCRPPGHHAGGDFMGGYCFLNNAAIATQAFLDQGARRVAILDVDYHHGNGTQDIFYRRDDVLFASIHGDPRVEYPYFLGYADERGEGAGEGCNHNYPLAHGSGWDLWSAALDDACVRIAGYAPDALVISLGVDTYKEDPISQFRLDSPDYLRMGERIARLGLPTLFIMEGGYAVEAIGINAVNVLQGYEGAAR
Protein: Phenolphthiocerol/phthiocerol polyketide synthase subunit B (EC 2.3.1.292) ((Phenol)carboxyphthiodiolenone synthase subunit B) (Beta-ketoacyl-acyl-carrier-protein synthase I) (Phthiocerol synthesis polyketide synthase type I PpsB) (Q7TXL9)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Part of the PpsABCDE complex involved in the biosynthesis of the lipid core common to phthiocerols and phenolphthiocerols by successive additions of malonyl-CoA or methylmalonyl-CoA extender units. PpsA can accept as substrate the activated forms of either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl from FadD29 (By similarity). PpsA initiates the biosynthesis and extends its substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the second and third malonyl-CoA extender units. PpsD adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product (By similarity).
Interaction partners:
Sequence:
MMRTAFSRISGMTAQQRTSLADEFDRVSRIAVAEPVAVVGIGCRFPGDVDGPESFWDFLVAGRNAISTVPADRWDAEAFYHPDPLTPGRMTTKWGGFVPDVAGFDAEFFGITPREAAAMDPQQRMLLEVAWEALEHAGIPPDSLGGTRTAVMMGVYFNEYQSMLAASPQNVDAYSGTGNAHSITVGRISYLLGLRGPAVAVDTACSSSLVAVHLACQSLRLRETDLALAGGVSITLRPETQIAISAWGLLSPQGRCAAFDAAADGFVRGEGAGVVVLKRLTDAVRDGDQVLAVVRGSAVNQDGRSNGVTAPNTAAQCDVIADALRSGDVAPDSVNYVEAHGTGTVLGDPIEFEALAATYGHGGDACALGAVKTNIGHLEAAAGIAGFIKATLAVQRATIPPNLHFSQWNPAIDAASTRFFVPTQNSPWPTAEGPRRAAVSSFGLGGTNAHVIIEQGSELAPVSEGGEDTGVSTLVVTGKTAQRMAATAQVLADWMEGPGAEVAVADVAHTVNHHRARQATFGTVVARDRAQAIAGLRALAAGQHAPGVVSHQDGSPGPGTVFVYSGRGSQWAGMGRQLLADEPAFAAAVAELEPVFVEQAGFSLRDVIATGKELVGIEQIQLGLIGMQLTLTELWRSYGVQPDLVIGHSMGEVAAAVVAGALTPAEGLRVTATRARLMAPLSGQGGMALLGLDAAATEALIADYPQVTVGIYNSPRQTVIAGPTEQIDELIARVRAQNRFASRVNIEVAPHNPAMDALQPAMRSELADLTPRTPTIGIISTTYADLHTQPIFDAEHWATNMRNPVRFQQAIASAGSGADGAYHTFIEISAHPLLTQAIADTLEDAHRPTKSAAKYLSIGTLQRDADDTVTFRTNLYTADIAHPPHTCHPPEPHPTIPTTPWQHTHHWIATTHPSTAAPEDPGSNKVVVNGQSTSESRALEDWCHQLAWPIRPAVSADPPSTAAWLVVADNELCHELARAADSRVDSLSPPALAAGSDPAALLDALRGVDNVLYAPPVPGELLDIESAYQVFHATRRLAAAMVASSATAISPPKLFIMTRNAQPISEGDRANPGHAVLWGLGRSLALEHPEIWGGIIDLDDSMPAELAVRHVLTAAHGTDGEDQVVYRSGARHVPRLQRRTLPGKPVTLNADASQLVIGATGNIGPHLIRQLARMGAKTIVAMARKPGALDELTQCLAATGTDLIAVAADATDPAAMQTLFDRFGTELPPLEGIYLAAFAGRPALLSEMTDDDVTTMFRPKLDALALLHRLSLKSPVRHFVLFSSVSGLLGSRWLAHYTATSAFLDSFAGARRTMGLPATVVDWGLWKSLADVQKDATQISAESGLQPMADEVAIGALPLVMNPDAAVATVVVAADWPLLAAAYRTRGALRIVDDLLPAPEDVGKGESEFRTSLRSCPAEKRRDMLFDHVGALAATVMGMPPTEPLDPSAGFFQLGMDSLMSVTLQRALSESLGEFLPASVVFDYPTVYSLTDYLATVLPELLEIGATAVATQQATDSYHELTEAELLEQLSERLRGTQ
Protein: Fibromodulin (FM) (Collagen-binding 59 kDa protein) (Keratan sulfate proteoglycan fibromodulin) (KSPG fibromodulin) (P50609)
Organism: Rattus norvegicus (Rat)
Function: Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Biglycan
- Transforming growth factor beta-2 proprotein
- Aggrecan core protein
- Decorin
- Lumican
- Tenomodulin
- Collagen alpha-1
- Osteomodulin
Sequence:
MQWASILLLRGLCSLSQGQYEEDSHWWLQYLRNQQSTYYDPYDTYPYETSDPYPYEVEEGPAYAYGAPPPPEPRDCPQECDCPPNFPTAMYCDNRNLKYLPFVPSRMKYVYFQNNQIAAIQEGVFDNATGLLWIALHGNQITSDKIGRKVFSKLRHLERLYLDHNNLTRMPGPLPRSLRELHLDHNQISRVPNNALEGLENLTALYLHHNEIQEVGSSMRGLRSLILLDLSYNHLRRVPDGLPSALEQLYLEHNNVYTVPDSYFRGSPKLLYVRLSHNSLTNNGLATNTFNSSSLLELDLSYNQLQKIPPVNTNLENLYLQGNRINEFSISSFCTVVDVMNFSKLQVLRLDGNEIKRSAMPVDAPLCLRLASLIEI
Protein: Neuroglobin (Nitrite reductase) (EC 1.7.-.-) (Q90YJ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in oxygen transport in the brain (By similarity). Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Capable of penetrating cell membranes.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ER97}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9ER97}. Note=Enriched in mitochondrial matrix upon oxygen-glucose deprivation (By similarity). Could have a membrane transducing activity allowing its translocation into cells (PubMed:18416560, PubMed:20417633). {ECO:0000250|UniProtKB:Q9ER97, ECO:0000269|PubMed:18416560, ECO:0000269|PubMed:20417633}.
Interaction partners:
- Myoglobin
- Cytoglobin-1
- Androglobin
- Cytochrome c
Sequence:
MEKLSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTNCGDAPECLSSPEFLEHVTKVMLVIDAAVSHLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGWAKNGEHKSN
Protein: Putrescine transport system permease protein PotH (P31135)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake. Responsible for the translocation of the substrate across the membrane (Probable). Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putrescine transport ATP-binding protein PotG
- Putrescine transport system permease protein PotI
- Spermidine/putrescine transport system permease protein PotC
- Putrescine-binding periplasmic protein PotF
- Spermidine/putrescine import ATP-binding protein PotA
- Spermidine/putrescine-binding periplasmic protein
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- sn-glycerol-3-phosphate transport system permease protein UgpE
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Inner membrane ABC transporter permease protein YdcV
Sequence:
MSTLEPAAQSKPPGGFKLWLSQLQMKHGRKLVIALPYIWLILLFLLPFLIVFKISLAEMARAIPPYTELMEWADGQLSITLNLGNFLQLTDDPLYFDAYLQSLQVAAISTFCCLLIGYPLAWAVAHSKPSTRNILLLLVILPSWTSFLIRVYAWMGILKNNGVLNNFLLWLGVIDQPLTILHTNLAVYIGIVYAYVPFMVLPIYTALIRIDYSLVEAALDLGARPLKTFFTVIVPLTKGGIIAGSMLVFIPAVGEFVIPELLGGPDSIMIGRVLWQEFFNNRDWPVASAVAIIMLLLLIVPIMWFHKHQQKSVGEHG