wanglab/gogpt-training-data huggingface dataset:
Protein: Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP) (Q9Y678)
Organism: Homo sapiens (Human)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11056392}. Golgi apparatus membrane {ECO:0000269|PubMed:11056392}; Peripheral membrane protein {ECO:0000269|PubMed:11056392}; Cytoplasmic side {ECO:0000269|PubMed:11056392}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit beta'
- Coatomer subunit alpha
- Coatomer subunit zeta-1
- Coatomer subunit epsilon
- Coatomer subunit zeta-2
- Coatomer subunit gamma-2
- Transmembrane emp24 domain-containing protein 10
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Sequence:
MLKKFDKKDEESGGGSNPFQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAIERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVNKMISKVTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTTNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLERALQQYTLEPSEKPFDLKSVPLATAPMAEQRTESTPITAVKQPEKVAATRQEIFQEQLAAVPEFRGLGPLFKSSPEPVALTESETEYVIRCTKHTFTNHMVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLCYVPARSLPYNQPGTCYTLVALPKEDPTAVACTFSCMMKFTVKDCDPTTGETDDEGYEDEYVLEDLEVTVADHIQKVMKLNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPDNKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSLEELPVDIILASVG
Protein: Disks large-associated protein 1 (DAP-1) (Guanylate kinase-associated protein) (rGKAP) (PSD-95/SAP90-binding protein 1) (SAP90/PSD-95-associated protein 1) (SAPAP1) (P97836)
Organism: Rattus norvegicus (Rat)
Function: Part of the postsynaptic scaffold in neuronal cells.
Subcellular location: Cell membrane; Peripheral membrane protein. Postsynaptic density. Synapse.
Interaction partners:
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains protein 3
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large homolog 2
- SH3 and multiple ankyrin repeat domains protein 2
- Glutamate receptor ionotropic, NMDA 2B
- Disks large homolog 3
- Glutamate receptor ionotropic, NMDA 2A
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Neuroligin-1
Sequence:
MKGLSGSRSHHHGITCESACDSLSHHSDHKPYLLSPVDHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDESALVPRTLATKANRLPTNLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGASKGGVNGGKASPDGSQTVRYGKRSKSKERRSEPKARSNASNASPTSPSWWSSDDNLDGDMCLYHTPSGVMTMGRCPDRSVSQYFMGAYNTISEQAVKASRSNNDVKCSTCANLPVTLDAPLLKKSAWSSTLTVSRAREVYQKASVNMDQAVVKSEACQQERSCQYLQVPQDEWTGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPMPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTGVIKLSSAVEVSSCITTYKKTPPPVPPRTTTKPFISITAQSSTESAQDAYMDGQGQRGDMISQSGLSNSTESLDSMKALTAAIEAANAQIHGPASQHMGSNAAAVTTTTTIATVTTEDRKKDFKKNRCLSIGIQVDDAEESEKMAESKTSSKFQSVGVQVEEEKCFRRFTRSNSVTTAVQADLDFHDNLENSLESIEDNSCPGPMARQFSRDASTSTVSIQGSGNHYHACAADDDFDTDFDPSILPPPDPWIDSITEDPLEAVQRSVCHRDGHWFLKLLQAERDRMEGWCKQMEREERENNLPEDILGKIRTAVGSAQLLMAQKFYQFRELCEENLNPNAHPRPTSQDLAGFWDMLQLSIENISMKFDELHQLKANNWKQMDPLDKKERRAPPPVPKKPAKGPAPLIRERSLESSQRQEARKRLMAAKRAASVRQNSATESAESIEIYIPEAQTRL
Protein: Armadillo repeat containing 6 (F5H2K4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSERCCSRYSSGASIGCTPTSTQAKMVSKRIAQETFDAAVRENIEEFAMGPEEAVKEAVEQFESQGVDLSNIVKTAPKVSADGSQEPTHDILQMLSDLQESVASSRPQEVSAYLTRFCDQCKQDKACRFLAAQKGAYPIIFTAWKLATAGDQGLLLQSLNALS
Protein: RanBP2-type domain-containing protein (Q38CA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRWLNIASNVFPLLRYRQVLGIKPPPPLHLSREGIWRKTEGLTSRTDGKGEITPADDLPPWPVDEIEFNTRAPMGGHDIRRAHEQQAAVLTGIDEDSGNLPSVSSTTHLSCLQPQRLTEEQKSEVRRVESTTEEGAGALEAGGWVCGSCLHCMPYRSRSVCDSCHTVRHDAATAVARWRGNPTTWFCSRCHEFNFERDAVCRCCNLAREAQTELHVAQHERVADEIQRSPVGSVIVTRNRVARWRCFVCSESNALQSSICRNCETGRFDLSVSCWNCGGQQKLSNSQLYGSEPADRIHVARPFGLHNCFPRLAPEQRCNRCRVPLHGATASTRSDAWLCGCGVVCNASLVSCTRCRIPRRFAHQSTLEELVRVWDFASATNWFCESCNHVNKSSRHVVALDRSCKNNSKSCPNGGTNLGTSGSFTDASVAKDASVKFARISHGTAKCERCGQKWHHQPVNDGQYWRCACHKVNKREDTRCQVCFLPAADGIRSDVLSFWSRGDWYCFNCQRQNYREKVVCACGEERPVDSRVDNKVAPAK
Protein: Vimentin (P09654)
Organism: Gallus gallus (Chicken)
Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08670}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}.
Interaction partners:
- Ubiquitin-associated domain-containing protein 1
- Caspase-3
- Desmin
- Alpha-actinin-2
- Caspase-7
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Zinc finger E-box-binding homeobox 1
- Cadherin-2
Sequence:
MSFTSSKNSSYRRMFGGGSRPSSGTRYITSSTRYSLGSALRPSSARYVSASPGGVYRTKATSVRLRSSMPPMRMHDAVDFTLADAINTEFKANRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGKGTSRLGDLYEEEMRDVRRQVDQLTNDKARVEVERDNLADDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLAGLDLERPVESLQEEIVFLKKLHDEEIRELQAQLQEQHIQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQEANEYRRQIQSLTCEVDALKGSNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRINMPIPTFASLNLRETNIESQPIVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
Protein: Cysteine-rich protein 1 (Zgc:103738 protein) (Q5BKV7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Serine palmitoyltransferase small subunit A
Sequence:
MPKCPKCQKEVYFAERVTSLGKDWHRPCLKCEKCNKTLSAGSHAEHEGKPYCNNPCYAALFGPKGFGRGGTESHTFK
Protein: (+)-alpha-terpineol synthase (EC 4.2.3.112) ((-)-limonene synthase) (EC 4.2.3.16) (Beta-bisabolene synthase) (EC 4.2.3.-) (Monoterpene synthase 1) (SaMonoTPS1) (F6M8I0)
Organism: Santalum album (White sandalwood)
Function: Monoterpene synthase which catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (R)-alpha-terpineol and (4S)-limonene, as well as small quantities of linalool, myrcene, (-)-alpha-pinene, (+)-sabinene and geraniol. To a lower extent, catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to beta-bisabolene.
Interaction partners:
Sequence:
MDAFATSPTSALIKAVNCIAHVTPMAGEDSSENRRASNYKPSSWDYEFLQSLATSHNTAQEKHMKMAEKLKEEVKSMIKGQMEPVAKLELINIVQRLGLKYRFESEIKEELLSLYKDGTDAWWVDNLHATALRFRLLRENGIFVPQDVFETFKDKSGKFKSQLCKDVRGLLSLYEASYLGWEGEDLLDEAKKFSTTNLNNVKESISSNTLGRLVKHALNLPLHWSAARYEARWFIDEYEKEENVNPNLLKYAKFDFNIVQSIHQRELGNLARWWVETGLDKLSFVRNTLMQNFMWGCAMVFEPQYGKVRDAAVKQASLIAMVDDVYDVYGSLEELEIFTDIVDRWDITGIDKLPRNISMILLTMFNTANQIGYDLLRDRGFNGIPHIAQAWATLCKKYLKEAKWYHSGYKPTLEEYLENGLVSISFVLSLVTAYLQTETLENLTYESAAYVNSVPPLVRYSGLLNRLYNDLGTSSAEIARGDTLKSIQCYMTQTGATEEAAREHIKGLVHEAWKGMNKCLFEQTPFAEPFVGFNVNTVRGSQFFYQHGDGYAVTESWTKDLSLSVLIHPIPLNEED
Protein: Probable endo-1,4-beta-xylanase B (Xylanase B) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase B) (Endo-1,4-beta-xylanase G1) (Xylanase G1) (P87037)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000269|PubMed:16672490}.
Interaction partners:
- Endo-1,4-beta-xylanase F1
- Exo-1,4-beta-xylosidase xlnD
- Xylanolytic transcriptional activator xlnR
- Probable alpha-glucuronidase A
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Endo-1,4-beta-xylanase F3
- Alpha-L-arabinofuranosidase B
- DNA-binding protein creA
- Probable endo-beta-1,4-glucanase B
- Probable feruloyl esterase A
Sequence:
MVSFSSLLLAVSAVSGALAAPGDSTLVELAKRAITSSETGTNNGYYYSFWTNGGGDVEYTNGNGGQYSVKWTNCDNFVAGKGWNPGSAKTVTYSGEWESNSNSYVSLYGWTQNPLVEYYIVDKYGDYDPSTGATELGTVESDGGTYKIYKTTRENAPSIEGTSTFNQYWSVRQSGRVGGTITAQNHFDAWANVGLQLGTHNYMILATEGYKSSGSATITVE
Protein: Auxin-responsive protein (F4IKE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004549}.
Interaction partners:
Sequence:
MSSGNDKIKQVLHIEDLMSYRLLSVDKDELVTSPCLKERNYLGLSDCSSVDSSTIPNVVGKSNLNFKATELRLGLPESQSPERETDFGLLSPRTPDEKLLFPLLPSKDNGSATTGHKNVVSGNKRGFADTWDEFSGVKGSVRPGGGINMMLSPKVKDVSKSIQEERSHAKGGLNNAPAAKAQVVGWPPIRSYRKNTMASSTSKNTDEVDGKPGLGVLFVKVSMDGAPYLRKVDLRTYTSYQQLSSALEKMFSCFTLGQCGLHGAQGRERMSEIKLKDLLHGSEFVLTYEDKDGDWMLVGDVPWEIFTETCQKLKIMKGSDSIGLAPGAVEKSKNKERV
Protein: Probable UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (UDP-glucose pyrophosphorylase) (UDPGP) (UGPase) (O59819)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphoglucomutase
- Galactose-1-phosphate uridylyltransferase
- Putative alpha,alpha-trehalose-phosphate synthase 106 kDa subunit
- Probable phosphoribomutase
- UDP-glucose 4-epimerase uge1
- Bifunctional protein gal10
- Alpha,alpha-trehalose-phosphate synthase
- Trehalose-phosphatase
- Trehalose-phosphatase
- 1,3-beta-glucan synthase component bgs3
Sequence:
MLHRRIHFKSQSTLDFDSVAVSISASTMKNELDKLVLNSRVSDKKTFGIQMDNFFALYRRYLLHTVKGYECDWDSIRPLGPEDMIDYGDLPLCKNAGKYLNRLAVVKLNGGMGNALGVNYPKAMIEVRDNQSFLDLSIRQIEYLNRRYDVSVPFILMNSYDTNDETCKVLRKYAGCKIDISTFEQSRYPRVFVDSQLPVPKAAPSPIEEWYPPGHGDIFDALVHSGTIERLLAQGKDYLFVSNIDNLGASVDLNILSHVIDNQIEYSMEITDKTKADIKVGILVNQDGLLRLLETNQVPEQHREEFMSDKVFKYINTNNVWLYLPAVKRVVENRELNLDIMPNIETVYYNNEPARIIEFTTAIGSAISQFKKTEGIRVSRPRFISVKNSSDLFLVRCDLYNVDHGSLKIEESRLGFPPPVVRMSNEFKDIAELFCRIPYMPSMKDLVSLSISGNVYFGRNVILKGNIVIVASENTILCIPSNAVLENCVVTGNCKIMEC
Protein: Afadin, adherens junction formation factor (J3KN01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPPKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKDDRPFQGEDVENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAEALEKYGLEKENPKDYCIARVMLPPGAQHSDEKGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDHIPKKTKKHLEGKTPKGKERADGSGYGSTLPPEKLPYLVELSPDGSDSRDKPKLYRLQLSVTEVGTEKLDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVEGQRISETTMLQSGMKVQFGASHVFKFVDPSQDHALAKRSVDGGLMVKGPRHKPGIVQETTFDLGGDIHSGTALPTSKSTTRLDSDRVSSASSTAERGMVKPMIRVEQQPDYRRQESRTQDASGPELILPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSNQYRPDISPTERTHKVIAVVNKMVSMMEGVIQEVDQVDQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYAPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVTVAENTADELARSDGREVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLIPHTRSPGTWTIYFEGADYESHLLRENTELAQPLRKEPEIITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSTQNGSPESPQLPWAEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSAYASGTTAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPPQNQWPNYEEKPHMHTDSNHSSIAIQRVTRSQEELREDKAYQLERHRIEAAMDRKSDSDMWINQSSSLDSSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAIPATPVAVSQPIRTDLPPPPPPPPVHYAGDFDGMSMDLPLPPPPSANQIGLPSAQVAAAERRKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPAPFSPLTAQQMKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITVSKEELSSGDSLSPDPWKRDAKEKLEKQQQMHIVDMLSKEIQELQSKPDRSAEESDRLRKLMLEWQFQKRLQESKQKDEDDEEEEDDDVDTMLIMQRLEAERRARLQDEERRRQQQLEEMRKREAEDRARQEEERRRQEEERTKRDAEEKRRQEEGYYSRLEAERRRQHDEAARRLLEPEAPGLCRPPLPRDYEPPSPSPAPGAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYNEEEEEEDCSLAGPNSYPGSTGAAVGAHDACRDAKEKRSKSQDADSPGSSGAPENLTFKERQRLFSQGQDVSNKVKASRKLTELENELNTK
Protein: Deoxyribonuclease-1-like 2 (EC 3.1.21.-) (DNase I homolog protein DHP1) (Deoxyribonuclease I-like 2) (DNase I-like 2) (Q92874)
Organism: Homo sapiens (Human)
Function: Divalent cation-dependent acid DNA endonuclease involved in the breakdown of the nucleus during corneocyte formation of epidermal keratinocytes. May play an immune role by eliminating harmful DNA released into the extracellular environment by damaged epidermal cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16902420}. Secreted {ECO:0000305}.
Interaction partners:
- 5'-3' exoribonuclease 2
- Decapping and exoribonuclease protein
- PHD finger protein 13
- Mitochondrial 2-oxodicarboxylate carrier
- T-box transcription factor TBX20
- Tight junction-associated protein 1
- ERI1 exoribonuclease 2
Sequence:
MGGPRALLAALWALEAAGTAALRIGAFNIQSFGDSKVSDPACGSIIAKILAGYDLALVQEVRDPDLSAVSALMEQINSVSEHEYSFVSSQPLGRDQYKEMYLFVYRKDAVSVVDTYLYPDPEDVFSREPFVVKFSAPGTGERAPPLPSRRALTPPPLPAAAQNLVLIPLHAAPHQAVAEIDALYDVYLDVIDKWGTDDMLFLGDFNADCSYVRAQDWAAIRLRSSEVFKWLIPDSADTTVGNSDCAYDRIVACGARLRRSLKPQSATVHDFQEEFGLDQTQALAISDHFPVEVTLKFHR
Protein: Pectin lyase-like superfamily protein (Polygalacturonase-like protein) (Q9LYJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Probable pectate lyase 20
- Probable pectate lyase 8
- Pectinesterase/pectinesterase inhibitor 3
- Beta-glucosidase 4
- GDP-mannose transporter GONST2
- Pectin lyase-like superfamily protein
- At5g48140
- Pectin lyase-like superfamily protein
- Exopolygalacturonase clone GBGA483
- Pectinesterase 2
Sequence:
MCRLTLKCLSLNFLLLISLFSSRFGTCDARYSVYWKGNRRSIAEGGSSGTINVLDHGAKGDGTSDDTKAFEDAWQVACKVAASTLLVPSGSTFLVGPVSFLGKECKEKIVFQLEGKIIAPTSASAWGSGLLQWIEFKALQGITIKGKGIIDGRGSVWWNDMMGTKMPRTKPTALRFYGSNGVTVSGITIQNSPQTHLKFDNCISIQVSDFTTSSPGDSPNTDGIHLQNSQDAVIYRSTLACGDDCISIQTGCSNINIHDVDCGPGHGISIGGLGKDNTKACVSNITVRDVTMHETTNGVRIKSWQGGSGSVKQVMFSNIQVSNVANPIIIDQYYCDGGGCHNETSAVAVSNINYINIKGTYTKEPVRFACSDSLPCTGISLSTIELKPATGKASSLDPFCWKAHGELKTKTLPPIQCLKTEKSPEAASRSNNDAC
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1 (F8VUB0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAARAGFQSVAPSGGAGASGGAGAAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQALWQYIKTHKLQDPHEREFVICDKYLQQIFESQRMKFSEIPQRLHALLMPPE
Protein: No extended memory, isoform L (EC 1.-.-.-, EC 1.16.1.7) (A0A0B4LF85)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKTRIKKRYEEDPDNAWNCCSWCEYLLIVILSTILLVGVLVLTLFWVMFYRDGFAWSESPKQQFNLHPILMIAGFVTLSGFSILIYRLCRCVKQIYVKLIHMFFHAVAIPCIALGFISVFASHDALHKVNFYSLHSWLGFVTMGMFVLQFVIGFFSFLVMLCCENKTYSCRSAMVPIHASLGLANFWLAIATSVTGLIEKERETVNEAGVSENKLVEHYITSAIGVTLIFIGIIVTFAVRRSNAPASAKVYVTERI
Protein: Phycocyanobilin lyase CpcS 1 (EC 4.-.-.-) (Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpcS) (Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpcS-III) (Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpeS) (Q8YZ70)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Catalyzes the site-selective attachment of phycocyanobilin (PCB) to 'Cys-82' in CpcB and 'Cys-83' in PecB. Also able to add PCB to ApcA1, ApcA2, ApcB, ApcD and ApcF, but not PecA. In vitro can be made to add phycoerythrobilin, a non-physiological substrate, to its target proteins (using genes from Fremyella diplosiphon PCC 7601). Binds PCB extremely rapidly, followed by a much slower phase of PCB transfer to the apo-acceptor protein. This suggests that the lyase has a chaperone-like function, and may serve to regulate the manner (possibly the conformation) in which the chromophore is attached to its target rather than to accelerate the rate.
Interaction partners:
- Phycocyanobilin lyase CpcT
- Bilin biosynthesis protein PecE
- Phycocyanobilin lyase subunit alpha
- Phycoerythrocyanin subunit beta
- C-phycocyanin beta subunit
- Phycocyanobilin lyase CpcT homolog
- Phycocyanobilin:ferredoxin oxidoreductase
- Phycocyanobilin lyase subunit beta
- Putative allophycocyanin subunit alpha 2
- Phycoerythrocyanin alpha chain
Sequence:
MNIEEFFELSAGKWFSHRTSHHLAFKQSEDGKSDLVIESLAADHPEVIKLCELYEVPASAASCGARVSWNGTMEWDEEKHTGSTVLATVPDVDNPNEGRLLREMGYAEKAPVAGRYKMGDDGALTLTTEYETMWSEERLWFASPNLRMRVSVLKRFGGFSMASFTSEIRMGGSPAAAKAEEAANSASS
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q9FFF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-protein hydrolase involved in the release of ubiquitin attached via both peptide and isopeptide linkages. Able to cleave 'Lys-48'-linked polyubiquitin chains. Involved in the direct or indirect regulation of AUX/IAA proteins stability (Probable). Acts as a linker between the TREX-2 complex and 26S proteasome.
Subcellular location: Nucleus {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}. Cytoplasm {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}.
Interaction partners:
- DNA-binding protein-like
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- RuvB-like protein 1
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Protein EIN6 ENHANCER
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- Proteasome subunit beta type-4
- Actin-related protein 4
Sequence:
MSWLPVESDPGIFTEIIQQMQVKGVQVEELYSLDFNSLDEIRPVYGLILLYKWRPEEKENRVVITEPNPNFFFASQIINNACATQAILSVLMNSSSIDIGSELSELKQFAKEFPPELKGLAINNNEAIRAAHNTFARPDPSSIMEDEELAAAKNLDEDDDVYHYISYLPVDGILYELDGLKEGPISLGQCLGEPEGIEWLRMVQPVVQEQIDRYSQNEIRFSLLAVVKNRKEMYVAELKEYQRKRERVLQQLGALQADKYAEKSSYEALDRELSEVNIGIETVSQKIVMEEEKSKNWKKENMRRKHNYVPFLFNFLKILADKKKLKPLIAKHHP
Protein: ORF2 (Q52878)
Organism: Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MASRNSARNTLMLAPVLDLNEATVLHERLLALKGGAVAIDASAVERVGALCVQVLMAAARSWEADRLSFTFAEVSDAFIKTTQLIGADIGPLMAKEI
Protein: Rho GTPase-activating protein 29 (PTPL1-associated RhoGAP protein 1) (Rho-type GTPase-activating protein 29) (Q52LW3)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis.
Interaction partners:
- Ras-related protein Rap-2a
- Ras-interacting protein 1
- Tyrosine-protein phosphatase non-receptor type 13
- Poly
- Transforming protein RhoA
- Cell division control protein 42 homolog
Sequence:
MIAHKQKKTKKKRAWASGQLSTDITTSEMGLKSLSSNSIFDPDYIKELVNDIRKFSHMLLYLKEAIFSDCFKEVIHIRLEELLRVLKSIMNKHQNLNSVDLQNAAEMLTAKVKAVNFTEVNEENKNDLFQEVFSSIETLAFTFGNILTNFLMGDVGNDSLLRLPVSRETKSFENVSVESVDSSSEKGNFSPLELDNVLLKNTDSIELALSYAKTWSKYTKNIVSWVEKKLNLELESTRNMVKLAEATRTNIGIQEFMPLQSLFTNALLNDIESSHLLQQTIAALQANKFVQPLLGRKNEMEKQRKEIKELWKQEQNKMLEAENALKKAKLLCMQRQDEYEKAKSSMFRAEEEHLSSSGGLAKNLNKQLEKKRRLEEEALQKVEEANELYKVCVTNVEERRNDLENTKREILAQLRTLVFQCDLTLKAVTVNLFHMQHLQAASLADSLQSLCDSAKLYDPGQEYSEFVKATNSTEEEKVDGNVNKHLNSSQPSGFGPANSLEDVVRLPDSSNKIEEDRCSNSADITGPSFIRSWTFGMFSDSESTGGSSESRSLDSESISPGDFHRKLPRTPSSGTMSSADDLDEREPPSPSETGPNSLGTFKKTLMSKAALTHKFRKLRSPTKCRDCEGIVVFQGVECEECLLVCHRKCLENLVIICGHQKLPGKIHLFGAEFTQVAKKEPDGIPFILKICASEIENRALCLQGIYRVCGNKIKTEKLCQALENGMHLVDISEFSSHDICDVLKLYLRQLPEPFILFRLYKEFIDLAKEIQHVNEEQETKKNSLEDKKWPNMCIEINRILLKSKDLLRQLPASNFNSLHFLIVHLKRVVDHAEENKMNSKNLGVIFGPSLIRPRPTTAPITISSLAEYSNQARLVEFLITYSQKIFDGSLQPQDVMCSIGVVDQGCFPKPLLSPEERDIERSMKSLFFSSKEDIHTSESESKIFERATSFEESERKQNALGKCDACLSDKAQLLLDQEAESASQKIEDGKTPKPLSLKSDRSTNNVERHTPRTKIRPVSLPVDRLLLASPPNERNGRNMGNVNLDKFCKNPAFEGVNRKDAATTVCSKFNGFDQQTLQKIQDKQYEQNSLTAKTTMIMPSALQEKGVTTSLQISGDHSINATQPSKPYAEPVRSVREASERRSSDSYPLAPVRAPRTLQPQHWTTFYKPHAPIISIRGNEEKPASPSAAVPPGTDHDPHGLVVKSMPDPDKASACPGQATGQPKEDSEELGLPDVNPMCQRPRLKRMQQFEDLEGEIPQFV
Protein: Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit (P0AAM1)
Organism: Escherichia coli (strain K12)
Function: Probable b-type cytochrome.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Hydrogenase 1 maturation protease
- Hydrogenase-1 small chain
- Hydrogenase-1 operon protein HyaF
- Hydrogenase-1 large chain
- Hydrogenase-1 operon protein HyaE
- Hydrogenase-2 large chain
- Hydrogenase-2 small chain
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Hydrogenase 2 maturation protease
Sequence:
MQQKSDNVVSHYVFEAPVRIWHWLTVLCMAVLMVTGYFIGKPLPSVSGEATYLFYMGYIRLIHFSAGMVFTVVLLMRIYWAFVGNRYSRELFIVPVWRKSWWQGVWYEIRWYLFLAKRPSADIGHNPIAQAAMFGYFLMSVFMIITGFALYSEHSQYAIFAPFRYVVEFFYWTGGNSMDIHSWHRLGMWLIGAFVIGHVYMALREDIMSDDTVISTMVNGYRSHKFGKISNKERS
Protein: Transcription factor MYBS1 (Myb-related protein S1) (OsMYBS1) (Syringolide-induced protein 1-3-1B) (Q8LH59)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that binds to 5'-TATCCA-3' elements in gene promoters. Derepresses strongly the sugar-repressed transcription of promoters containing SRS or 5'-TATCCA-3' elements. Functions with GAMYB to integrate diverse nutrient starvation and gibberellin (GA) signaling pathways during germination of grains. Sugar, nitrogen and phosphate starvation signals converge and interconnect with GA to promote the co-nuclear import of MYBS1 and GAMYB, resulting in the expression of a large set of GA-inducible hydrolases, transporters, and regulators that are essential for mobilization of nutrient reserves in the endosperm to support seedling growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:22773748}. Cytoplasm {ECO:0000269|PubMed:22773748}. Note=Preferentially localized to the nucleus under sugar starvation conditions. Glucose inhibits nuclear localization. {ECO:0000269|PubMed:22773748}.
Interaction partners:
Sequence:
MTSQAATTTTTAAAAAAWTREDDKAFENALAACAAPPPADGGAPDDDWFAALAASVPGARSAEEVRRHYEALVEDVAAIDAGRVPLPRYAGEESAAPPDGAGAAAAASKDGGHRRDERKGGGGGYDGGKSCSKAEQERRKGIPWTEEEHRLFLLGLDKFGKGDWRSISRNFVISRTPTQVASHAQKYFIRLNSMNRDRRRSSIHDITSVTAGDQVAAQQGAPITGHQATGNPAAAALGPPGMKHHHHHHPGGAPPPMPMYSAAPMGHPVAGHMVPAAVGTPVVFPPGHAPYVVPVGYPAPPAKMHQ